Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 01:58, 15 November 2007 (UTC)[edit]
Proteins without matches (8)[edit]
Proteins with a High Potential Match (9)[edit]
Redirected Proteins (8)[edit]
Manual Inspection (Page not found) (17)[edit]
Updated (8)[edit]
Protein Status Grid - Date: 01:58, 15 November 2007 (UTC)[edit]
Vebose Log - Date: 01:58, 15 November 2007 (UTC)[edit]
- INFO: Beginning work on ADA... {November 14, 2007 5:34:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:34:59 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ADA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1krm.
| PDB = {{PDB2|1krm}}, {{PDB2|1ndv}}, {{PDB2|1ndw}}, {{PDB2|1ndy}}, {{PDB2|1ndz}}, {{PDB2|1o5r}}, {{PDB2|1qxl}}, {{PDB2|1uml}}, {{PDB2|1v79}}, {{PDB2|1v7a}}, {{PDB2|1vfl}}, {{PDB2|1w1i}}, {{PDB2|1wxy}}, {{PDB2|1wxz}}, {{PDB2|2bgn}}, {{PDB2|2e1w}}
| Name = Adenosine deaminase
| HGNCid = 186
| Symbol = ADA
| AltSymbols =;
| OMIM = 608958
| ECnumber =
| Homologene = 37249
| MGIid = 87916
| GeneAtlas_image1 = PBB_GE_ADA_204639_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADA_216705_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004000 |text = adenosine deaminase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006163 |text = purine nucleotide metabolic process}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0009168 |text = purine ribonucleoside monophosphate biosynthetic process}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 100
| Hs_Ensembl = ENSG00000196839
| Hs_RefseqProtein = NP_000013
| Hs_RefseqmRNA = NM_000022
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 42681577
| Hs_GenLoc_end = 42713797
| Hs_Uniprot = P00813
| Mm_EntrezGene = 11486
| Mm_Ensembl = ENSMUSG00000017697
| Mm_RefseqmRNA = NM_007398
| Mm_RefseqProtein = NP_031424
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 163418025
| Mm_GenLoc_end = 163441618
| Mm_Uniprot = Q4FJZ7
}}
}}
'''Adenosine deaminase''', also known as '''ADA''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Adenosine deaminase catalyzes the hydrolysis of adenosine to inosine. ADA deficiency causes one form of severe combined immunodeficiency disease (SCID), in which there is dysfunction of both B and T lymphocytes with impaired cellular immunity and decreased production of immunoglobulins.<ref>{{cite web | title = Entrez Gene: ADA adenosine deaminase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=100| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=da Cunha JG |title=[Adenosine deaminase. A pluridisciplinary enzyme] |journal=Acta médica portuguesa |volume=4 |issue= 6 |pages= 315-23 |year= 1992 |pmid= 1807098 |doi= }}
*{{cite journal | author=Franco R, Casadó V, Ciruela F, ''et al.'' |title=Cell surface adenosine deaminase: much more than an ectoenzyme. |journal=Prog. Neurobiol. |volume=52 |issue= 4 |pages= 283-94 |year= 1997 |pmid= 9247966 |doi= }}
*{{cite journal | author=Valenzuela A, Blanco J, Callebaut C, ''et al.'' |title=HIV-1 envelope gp120 and viral particles block adenosine deaminase binding to human CD26. |journal=Adv. Exp. Med. Biol. |volume=421 |issue= |pages= 185-92 |year= 1997 |pmid= 9330696 |doi= }}
*{{cite journal | author=Moriwaki Y, Yamamoto T, Higashino K |title=Enzymes involved in purine metabolism--a review of histochemical localization and functional implications. |journal=Histol. Histopathol. |volume=14 |issue= 4 |pages= 1321-40 |year= 1999 |pmid= 10506947 |doi= }}
*{{cite journal | author=Hirschhorn R |title=Identification of two new missense mutations (R156C and S291L) in two ADA- SCID patients unusual for response to therapy with partial exchange transfusions. |journal=Hum. Mutat. |volume=1 |issue= 2 |pages= 166-8 |year= 1993 |pmid= 1284479 |doi= 10.1002/humu.1380010214 }}
*{{cite journal | author=Berkvens TM, van Ormondt H, Gerritsen EJ, ''et al.'' |title=Identical 3250-bp deletion between two AluI repeats in the ADA genes of unrelated ADA-SCID patients. |journal=Genomics |volume=7 |issue= 4 |pages= 486-90 |year= 1990 |pmid= 1696926 |doi= }}
*{{cite journal | author=Aran JM, Colomer D, Matutes E, ''et al.'' |title=Presence of adenosine deaminase on the surface of mononuclear blood cells: immunochemical localization using light and electron microscopy. |journal=J. Histochem. Cytochem. |volume=39 |issue= 8 |pages= 1001-8 |year= 1991 |pmid= 1856451 |doi= }}
*{{cite journal | author=Bielat K, Tritsch GL |title=Ecto-enzyme activity of human erythrocyte adenosine deaminase. |journal=Mol. Cell. Biochem. |volume=86 |issue= 2 |pages= 135-42 |year= 1989 |pmid= 2770711 |doi= }}
*{{cite journal | author=Hirschhorn R, Tzall S, Ellenbogen A, Orkin SH |title=Identification of a point mutation resulting in a heat-labile adenosine deaminase (ADA) in two unrelated children with partial ADA deficiency. |journal=J. Clin. Invest. |volume=83 |issue= 2 |pages= 497-501 |year= 1989 |pmid= 2783588 |doi= }}
*{{cite journal | author=Murray JL, Perez-Soler R, Bywaters D, Hersh EM |title=Decreased adenosine deaminase (ADA) and 5'nucleotidase (5NT) activity in peripheral blood T cells in Hodgkin disease. |journal=Am. J. Hematol. |volume=21 |issue= 1 |pages= 57-66 |year= 1986 |pmid= 3010705 |doi= }}
*{{cite journal | author=Wiginton DA, Kaplan DJ, States JC, ''et al.'' |title=Complete sequence and structure of the gene for human adenosine deaminase. |journal=Biochemistry |volume=25 |issue= 25 |pages= 8234-44 |year= 1987 |pmid= 3028473 |doi= }}
*{{cite journal | author=Akeson AL, Wiginton DA, Dusing MR, ''et al.'' |title=Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts. |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 16291-6 |year= 1988 |pmid= 3182793 |doi= }}
*{{cite journal | author=Glader BE, Backer K |title=Elevated red cell adenosine deaminase activity: a marker of disordered erythropoiesis in Diamond-Blackfan anaemia and other haematologic diseases. |journal=Br. J. Haematol. |volume=68 |issue= 2 |pages= 165-8 |year= 1988 |pmid= 3348976 |doi= }}
*{{cite journal | author=Petersen MB, Tranebjaerg L, Tommerup N, ''et al.'' |title=New assignment of the adenosine deaminase gene locus to chromosome 20q13 X 11 by study of a patient with interstitial deletion 20q. |journal=J. Med. Genet. |volume=24 |issue= 2 |pages= 93-6 |year= 1987 |pmid= 3560174 |doi= }}
*{{cite journal | author=Orkin SH, Goff SC, Kelley WN, Daddona PE |title=Transient expression of human adenosine deaminase cDNAs: identification of a nonfunctional clone resulting from a single amino acid substitution. |journal=Mol. Cell. Biol. |volume=5 |issue= 4 |pages= 762-7 |year= 1985 |pmid= 3838797 |doi= }}
*{{cite journal | author=Valerio D, Duyvesteyn MG, Dekker BM, ''et al.'' |title=Adenosine deaminase: characterization and expression of a gene with a remarkable promoter. |journal=EMBO J. |volume=4 |issue= 2 |pages= 437-43 |year= 1985 |pmid= 3839456 |doi= }}
*{{cite journal | author=Bonthron DT, Markham AF, Ginsburg D, Orkin SH |title=Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency. |journal=J. Clin. Invest. |volume=76 |issue= 2 |pages= 894-7 |year= 1985 |pmid= 3839802 |doi= }}
*{{cite journal | author=Daddona PE, Shewach DS, Kelley WN, ''et al.'' |title=Human adenosine deaminase. cDNA and complete primary amino acid sequence. |journal=J. Biol. Chem. |volume=259 |issue= 19 |pages= 12101-6 |year= 1984 |pmid= 6090454 |doi= }}
*{{cite journal | author=Valerio D, Duyvesteyn MG, Meera Khan P, ''et al.'' |title=Isolation of cDNA clones for human adenosine deaminase. |journal=Gene |volume=25 |issue= 2-3 |pages= 231-40 |year= 1984 |pmid= 6198240 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ANG... {November 14, 2007 5:34:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:35:28 PM PST}
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{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ANG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a4y.
| PDB = {{PDB2|1a4y}}, {{PDB2|1ang}}, {{PDB2|1awz}}, {{PDB2|1b1e}}, {{PDB2|1b1i}}, {{PDB2|1b1j}}, {{PDB2|1h0d}}, {{PDB2|1h52}}, {{PDB2|1h53}}, {{PDB2|1hby}}, {{PDB2|1k58}}, {{PDB2|1k59}}, {{PDB2|1k5a}}, {{PDB2|1k5b}}, {{PDB2|1un3}}, {{PDB2|1un4}}, {{PDB2|1un5}}, {{PDB2|2ang}}
| Name = Angiogenin, ribonuclease, RNase A family, 5
| HGNCid = 483
| Symbol = ANG
| AltSymbols =; MGC71966; RNASE4; RNASE5
| OMIM = 105850
| ECnumber =
| Homologene = 74385
| MGIid = 88022
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004522 |text = pancreatic ribonuclease activity}} {{GNF_GO|id=GO:0004540 |text = ribonuclease activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0019843 |text = rRNA binding}}
| Component = {{GNF_GO|id=GO:0005605 |text = basal lamina}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0032311 |text = angiogenin-PRI complex}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0001890 |text = placenta development}} {{GNF_GO|id=GO:0001938 |text = positive regulation of endothelial cell proliferation}} {{GNF_GO|id=GO:0006651 |text = diacylglycerol biosynthetic process}} {{GNF_GO|id=GO:0007154 |text = cell communication}} {{GNF_GO|id=GO:0007202 |text = phospholipase C activation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009303 |text = rRNA transcription}} {{GNF_GO|id=GO:0017148 |text = negative regulation of protein biosynthetic process}} {{GNF_GO|id=GO:0030041 |text = actin filament polymerization}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0032431 |text = activation of phospholipase A2}} {{GNF_GO|id=GO:0042592 |text = homeostatic process}} {{GNF_GO|id=GO:0048662 |text = negative regulation of smooth muscle cell proliferation}} {{GNF_GO|id=GO:0050714 |text = positive regulation of protein secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 283
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001136
| Hs_RefseqmRNA = NM_001145
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 11727
| Mm_Ensembl = ENSMUSG00000072115
| Mm_RefseqmRNA = NM_007447
| Mm_RefseqProtein = NP_031473
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 50018364
| Mm_GenLoc_end = 50023962
| Mm_Uniprot = Q3TBG7
}}
}}
'''Angiogenin, ribonuclease, RNase A family, 5''', also known as '''ANG''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is an exceedingly potent mediator of new blood vessel formation. It hydrolyzes cellular tRNAs resulting in decreased protein synthesis and is similar to pancreatic ribonuclease. Alternative splicing results in two transcript variants encoding the same protein. This gene and the gene that encodes ribonuclease, RNase A family, 4 share promoters and 5' exons. Each gene splices to a unique downstream exon that contains its complete coding region.<ref>{{cite web | title = Entrez Gene: ANG angiogenin, ribonuclease, RNase A family, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=283| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Saxena SK, Rybak SM, Davey RT, ''et al.'' |title=Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. |journal=J. Biol. Chem. |volume=267 |issue= 30 |pages= 21982-6 |year= 1992 |pmid= 1400510 |doi= }}
*{{cite journal | author=Weremowicz S, Fox EA, Morton CC, Vallee BL |title=Localization of the human angiogenin gene to chromosome band 14q11, proximal to the T cell receptor alpha/delta locus. |journal=Am. J. Hum. Genet. |volume=47 |issue= 6 |pages= 973-81 |year= 1990 |pmid= 1978563 |doi= }}
*{{cite journal | author=Weremowicz S, Fox EA, Morton CC, Vallee BL |title=The placental ribonuclease inhibitor (RNH) gene is located on chromosome subband 11p15.5. |journal=Genomics |volume=8 |issue= 4 |pages= 717-21 |year= 1991 |pmid= 2276743 |doi= }}
*{{cite journal | author=Shapiro R, Riordan JF, Vallee BL |title=Characteristic ribonucleolytic activity of human angiogenin. |journal=Biochemistry |volume=25 |issue= 12 |pages= 3527-32 |year= 1986 |pmid= 2424496 |doi= }}
*{{cite journal | author=Weiner HL, Weiner LH, Swain JL |title=Tissue distribution and developmental expression of the messenger RNA encoding angiogenin. |journal=Science |volume=237 |issue= 4812 |pages= 280-2 |year= 1987 |pmid= 2440105 |doi= }}
*{{cite journal | author=Bicknell R, Vallee BL |title=Angiogenin activates endothelial cell phospholipase C. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 16 |pages= 5961-5 |year= 1988 |pmid= 2457905 |doi= }}
*{{cite journal | author=Shapiro R, Vallee BL |title=Site-directed mutagenesis of histidine-13 and histidine-114 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis. |journal=Biochemistry |volume=28 |issue= 18 |pages= 7401-8 |year= 1990 |pmid= 2479414 |doi= }}
*{{cite journal | author=Bicknell R, Vallee BL |title=Angiogenin stimulates endothelial cell prostacyclin secretion by activation of phospholipase A2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 5 |pages= 1573-7 |year= 1989 |pmid= 2646638 |doi= }}
*{{cite journal | author=Lee FS, Vallee BL |title=Characterization of ribonucleolytic activity of angiogenin towards tRNA. |journal=Biochem. Biophys. Res. Commun. |volume=161 |issue= 1 |pages= 121-6 |year= 1989 |pmid= 2730651 |doi= }}
*{{cite journal | author=Lee FS, Vallee BL |title=Binding of placental ribonuclease inhibitor to the active site of angiogenin. |journal=Biochemistry |volume=28 |issue= 8 |pages= 3556-61 |year= 1989 |pmid= 2742853 |doi= }}
*{{cite journal | author=Strydom DJ, Fett JW, Lobb RR, ''et al.'' |title=Amino acid sequence of human tumor derived angiogenin. |journal=Biochemistry |volume=24 |issue= 20 |pages= 5486-94 |year= 1986 |pmid= 2866794 |doi= }}
*{{cite journal | author=Kurachi K, Davie EW, Strydom DJ, ''et al.'' |title=Sequence of the cDNA and gene for angiogenin, a human angiogenesis factor. |journal=Biochemistry |volume=24 |issue= 20 |pages= 5494-9 |year= 1986 |pmid= 2866795 |doi= }}
*{{cite journal | author=Shapiro R, Vallee BL |title=Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 8 |pages= 2238-41 |year= 1987 |pmid= 3470787 |doi= }}
*{{cite journal | author=Rybak SM, Fett JW, Yao QZ, Vallee BL |title=Angiogenin mRNA in human tumor and normal cells. |journal=Biochem. Biophys. Res. Commun. |volume=146 |issue= 3 |pages= 1240-8 |year= 1987 |pmid= 3619929 |doi= }}
*{{cite journal | author=Shapiro R, Strydom DJ, Olson KA, Vallee BL |title=Isolation of angiogenin from normal human plasma. |journal=Biochemistry |volume=26 |issue= 16 |pages= 5141-6 |year= 1987 |pmid= 3663649 |doi= }}
*{{cite journal | author=Hu GF, Strydom DJ, Fett JW, ''et al.'' |title=Actin is a binding protein for angiogenin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 4 |pages= 1217-21 |year= 1993 |pmid= 7679494 |doi= }}
*{{cite journal | author=Moroianu J, Riordan JF |title=Identification of the nucleolar targeting signal of human angiogenin. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 3 |pages= 1765-72 |year= 1994 |pmid= 7945327 |doi= 10.1006/bbrc.1994.2391 }}
*{{cite journal | author=Moroianu J, Riordan JF |title=Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 5 |pages= 1677-81 |year= 1994 |pmid= 8127865 |doi= }}
*{{cite journal | author=Acharya KR, Shapiro R, Allen SC, ''et al.'' |title=Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 2915-9 |year= 1994 |pmid= 8159679 |doi= }}
*{{cite journal | author=Hu GF, Riordan JF, Vallee BL |title=A putative angiogenin receptor in angiogenin-responsive human endothelial cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 6 |pages= 2204-9 |year= 1997 |pmid= 9122172 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ANXA1... {November 14, 2007 5:35:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:35:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ANXA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ain.
| PDB = {{PDB2|1ain}}, {{PDB2|1bo9}}
| Name = Annexin A1
| HGNCid = 533
| Symbol = ANXA1
| AltSymbols =; ANX1; LPC1
| OMIM = 151690
| ECnumber =
| Homologene = 563
| MGIid = 96819
| GeneAtlas_image1 = PBB_GE_ANXA1_201012_at_tn.png
| Function = {{GNF_GO|id=GO:0004859 |text = phospholipase inhibitor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005544 |text = calcium-dependent phospholipid binding}} {{GNF_GO|id=GO:0019834 |text = phospholipase A2 inhibitor activity}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0001533 |text = cornified envelope}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0042383 |text = sarcolemma}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0018149 |text = peptide cross-linking}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0050482 |text = arachidonic acid secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 301
| Hs_Ensembl = ENSG00000135046
| Hs_RefseqProtein = NP_000691
| Hs_RefseqmRNA = NM_000700
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 74956493
| Hs_GenLoc_end = 74975129
| Hs_Uniprot = P04083
| Mm_EntrezGene = 16952
| Mm_Ensembl = ENSMUSG00000024659
| Mm_RefseqmRNA = NM_010730
| Mm_RefseqProtein = NP_034860
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 20440453
| Mm_GenLoc_end = 20457696
| Mm_Uniprot = Q3U5N9
}}
}}
'''Annexin A1''', also known as '''ANXA1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Annexin I belongs to a family of Ca(2+)-dependent phospholipid binding proteins which have a molecular weight of approximately 35,000 to 40,000 and are preferentially located on the cytosolic face of the plasma membrane. Annexin I protein has an apparent relative molecular mass of 40 kDa, with phospholipase A2 inhibitory activity. Since phospholipase A2 is required for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, annexin I may have potential anti-inflammatory activity.<ref>{{cite web | title = Entrez Gene: ANXA1 annexin A1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=301| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Crompton MR, Moss SE, Crumpton MJ |title=Diversity in the lipocortin/calpactin family. |journal=Cell |volume=55 |issue= 1 |pages= 1-3 |year= 1988 |pmid= 2971450 |doi= }}
*{{cite journal | author=Lim LH, Pervaiz S |title=Annexin 1: the new face of an old molecule. |journal=FASEB J. |volume=21 |issue= 4 |pages= 968-75 |year= 2007 |pmid= 17215481 |doi= 10.1096/fj.06-7464rev }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Ando Y, Imamura S, Owada MK, Kannagi R |title=Calcium-induced intracellular cross-linking of lipocortin I by tissue transglutaminase in A431 cells. Augmentation by membrane phospholipids. |journal=J. Biol. Chem. |volume=266 |issue= 2 |pages= 1101-8 |year= 1991 |pmid= 1670773 |doi= }}
*{{cite journal | author=Kovacic RT, Tizard R, Cate RL, ''et al.'' |title=Correlation of gene and protein structure of rat and human lipocortin I. |journal=Biochemistry |volume=30 |issue= 37 |pages= 9015-21 |year= 1991 |pmid= 1832554 |doi= }}
*{{cite journal | author=Varticovski L, Chahwala SB, Whitman M, ''et al.'' |title=Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C. |journal=Biochemistry |volume=27 |issue= 10 |pages= 3682-90 |year= 1988 |pmid= 2457390 |doi= }}
*{{cite journal | author=Pepinsky RB, Sinclair LK, Chow EP, O'Brine-Greco B |title=A dimeric form of lipocortin-1 in human placenta. |journal=Biochem. J. |volume=263 |issue= 1 |pages= 97-103 |year= 1990 |pmid= 2532504 |doi= }}
*{{cite journal | author=Wallner BP, Mattaliano RJ, Hession C, ''et al.'' |title=Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity. |journal=Nature |volume=320 |issue= 6057 |pages= 77-81 |year= 1986 |pmid= 2936963 |doi= 10.1038/320077a0 }}
*{{cite journal | author=Kaplan R, Jaye M, Burgess WH, ''et al.'' |title=Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein. |journal=J. Biol. Chem. |volume=263 |issue= 17 |pages= 8037-43 |year= 1988 |pmid= 2967291 |doi= }}
*{{cite journal | author=Huebner K, Cannizzaro LA, Frey AZ, ''et al.'' |title=Chromosomal localization of the human genes for lipocortin I and lipocortin II. |journal=Oncogene Res. |volume=2 |issue= 4 |pages= 299-310 |year= 1988 |pmid= 2969496 |doi= }}
*{{cite journal | author=Biemann K, Scoble HA |title=Characterization by tandem mass spectrometry of structural modifications in proteins. |journal=Science |volume=237 |issue= 4818 |pages= 992-8 |year= 1987 |pmid= 3303336 |doi= }}
*{{cite journal | author=Arcone R, Arpaia G, Ruoppolo M, ''et al.'' |title=Structural characterization of a biologically active human lipocortin 1 expressed in Escherichia coli. |journal=Eur. J. Biochem. |volume=211 |issue= 1-2 |pages= 347-55 |year= 1993 |pmid= 8425544 |doi= }}
*{{cite journal | author=Weng X, Luecke H, Song IS, ''et al.'' |title=Crystal structure of human annexin I at 2.5 A resolution. |journal=Protein Sci. |volume=2 |issue= 3 |pages= 448-58 |year= 1993 |pmid= 8453382 |doi= }}
*{{cite journal | author=Mailliard WS, Haigler HT, Schlaepfer DD |title=Calcium-dependent binding of S100C to the N-terminal domain of annexin I. |journal=J. Biol. Chem. |volume=271 |issue= 2 |pages= 719-25 |year= 1996 |pmid= 8557678 |doi= }}
*{{cite journal | author=Morgan RO, Fernández MP |title=A BC200-derived element and Z-DNA as structural markers in annexin I genes: relevance to Alu evolution and annexin tetrad formation. |journal=J. Mol. Evol. |volume=41 |issue= 6 |pages= 979-85 |year= 1996 |pmid= 8587144 |doi= }}
*{{cite journal | author=Almawi WY, Saouda MS, Stevens AC, ''et al.'' |title=Partial mediation of glucocorticoid antiproliferative effects by lipocortins. |journal=J. Immunol. |volume=157 |issue= 12 |pages= 5231-9 |year= 1997 |pmid= 8955167 |doi= }}
*{{cite journal | author=Croxtall JD, Wu HL, Yang HY, ''et al.'' |title=Lipocortin 1 co-associates with cytokeratins 8 and 18 in A549 cells via the N-terminal domain. |journal=Biochim. Biophys. Acta |volume=1401 |issue= 1 |pages= 39-51 |year= 1998 |pmid= 9459484 |doi= }}
*{{cite journal | author=Gao J, Li Y, Yan H |title=NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit. |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 2971-7 |year= 1999 |pmid= 9915835 |doi= }}
*{{cite journal | author=Manda R, Kohno T, Matsuno Y, ''et al.'' |title=Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. |journal=Genomics |volume=61 |issue= 1 |pages= 5-14 |year= 1999 |pmid= 10512675 |doi= 10.1006/geno.1999.5939 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AURKB... {November 14, 2007 5:50:47 PM PST}
- SEARCH REDIRECT: Control Box Found: AURKB {November 14, 2007 5:51:29 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:51:32 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:51:32 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:51:32 PM PST}
- UPDATED: Updated protein page: AURKB {November 14, 2007 5:51:39 PM PST}
- INFO: Beginning work on CASP6... {November 14, 2007 5:35:55 PM PST}
- SEARCH REDIRECT: Control Box Found: CASP6 {November 14, 2007 5:36:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:36:29 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:36:29 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:36:29 PM PST}
- UPDATED: Updated protein page: CASP6 {November 14, 2007 5:36:35 PM PST}
- INFO: Beginning work on CD2... {November 14, 2007 5:36:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:37:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CD2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cdb.
| PDB = {{PDB2|1cdb}}, {{PDB2|1gya}}, {{PDB2|1hnf}}, {{PDB2|1qa9}}
| Name = CD2 molecule
| HGNCid = 1639
| Symbol = CD2
| AltSymbols =; SRBC; T11
| OMIM = 186990
| ECnumber =
| Homologene = 1338
| MGIid = 88320
| GeneAtlas_image1 = PBB_GE_CD2_205831_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001766 |text = lipid raft polarization}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030101 |text = natural killer cell activation}} {{GNF_GO|id=GO:0030887 |text = positive regulation of myeloid dendritic cell activation}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0045580 |text = regulation of T cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 914
| Hs_Ensembl = ENSG00000116824
| Hs_RefseqProtein = NP_001758
| Hs_RefseqmRNA = NM_001767
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 117098530
| Hs_GenLoc_end = 117113373
| Hs_Uniprot = P06729
| Mm_EntrezGene = 12481
| Mm_Ensembl = ENSMUSG00000027863
| Mm_RefseqmRNA = NM_013486
| Mm_RefseqProtein = NP_038514
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 101404969
| Mm_GenLoc_end = 101417000
| Mm_Uniprot = Q5SRC1
}}
}}
'''CD2 molecule''', also known as '''CD2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sayre PH, Reinherz EL |title=Structure and function of the erythrocyte receptor CD2 on human T lymphocytes: a review. |journal=Scand. J. Rheumatol. Suppl. |volume=76 |issue= |pages= 131-44 |year= 1989 |pmid= 2471997 |doi= }}
*{{cite journal | author=Rouleau M, Mollereau B, Bernard A, ''et al.'' |title=CD2 induced apoptosis of peripheral T cells. |journal=Transplant. Proc. |volume=29 |issue= 5 |pages= 2377-8 |year= 1997 |pmid= 9270771 |doi= }}
*{{cite journal | author=Lüscher B |title=Function and regulation of the transcription factors of the Myc/Max/Mad network. |journal=Gene |volume=277 |issue= 1-2 |pages= 1-14 |year= 2001 |pmid= 11602341 |doi= }}
*{{cite journal | author=Yang JJ, Ye Y, Carroll A, ''et al.'' |title=Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation. |journal=Curr. Protein Pept. Sci. |volume=2 |issue= 1 |pages= 1-17 |year= 2002 |pmid= 12369898 |doi= }}
*{{cite journal | author=Bell GM, Seaman WE, Niemi EC, Imboden JB |title=The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. |journal=J. Exp. Med. |volume=175 |issue= 2 |pages= 527-36 |year= 1992 |pmid= 1346273 |doi= }}
*{{cite journal | author=Marie-Cardine A, Maridonneau-Parini I, Ferrer M, ''et al.'' |title=The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2. |journal=J. Immunol. |volume=148 |issue= 12 |pages= 3879-84 |year= 1992 |pmid= 1351089 |doi= }}
*{{cite journal | author=Hahn WC, Menu E, Bothwell AL, ''et al.'' |title=Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59. |journal=Science |volume=256 |issue= 5065 |pages= 1805-7 |year= 1992 |pmid= 1377404 |doi= }}
*{{cite journal | author=Luzzati AL, Giacomini E, Giordani L, ''et al.'' |title=The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope. |journal=Immunol. Lett. |volume=33 |issue= 3 |pages= 307-14 |year= 1992 |pmid= 1385321 |doi= }}
*{{cite journal | author=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |doi= }}
*{{cite journal | author=Schraven B, Samstag Y, Altevogt P, Meuer SC |title=Association of CD2 and CD45 on human T lymphocytes. |journal=Nature |volume=345 |issue= 6270 |pages= 71-4 |year= 1990 |pmid= 1970422 |doi= 10.1038/345071a0 }}
*{{cite journal | author=Samelson LE, Fletcher MC, Ledbetter JA, June CH |title=Activation of tyrosine phosphorylation in human T cells via the CD2 pathway. Regulation by the CD45 tyrosine phosphatase. |journal=J. Immunol. |volume=145 |issue= 8 |pages= 2448-54 |year= 1990 |pmid= 1976695 |doi= }}
*{{cite journal | author=Luzzati AL, Pugliese O, Giacomini E, ''et al.'' |title=Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV. |journal=Folia Biol. (Praha) |volume=36 |issue= 1 |pages= 71-7 |year= 1990 |pmid= 2111780 |doi= }}
*{{cite journal | author=Seed B, Aruffo A |title=Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 10 |pages= 3365-9 |year= 1987 |pmid= 2437578 |doi= }}
*{{cite journal | author=Peterson A, Seed B |title=Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2). |journal=Nature |volume=329 |issue= 6142 |pages= 842-6 |year= 1987 |pmid= 2444890 |doi= 10.1038/329842a0 }}
*{{cite journal | author=Sayre PH, Chang HC, Hussey RE, ''et al.'' |title=Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 9 |pages= 2941-5 |year= 1987 |pmid= 2883656 |doi= }}
*{{cite journal | author=Diamond DJ, Clayton LK, Sayre PH, Reinherz EL |title=Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 5 |pages= 1615-9 |year= 1988 |pmid= 2894031 |doi= }}
*{{cite journal | author=Lang G, Wotton D, Owen MJ, ''et al.'' |title=The structure of the human CD2 gene and its expression in transgenic mice. |journal=EMBO J. |volume=7 |issue= 6 |pages= 1675-82 |year= 1988 |pmid= 2901953 |doi= }}
*{{cite journal | author=Leca G, Boumsell L, Fabbi M, ''et al.'' |title=The sheep erythrocyte receptor and both alpha and beta chains of the human T-lymphocyte antigen receptor bind the mitogenic lectin (phytohaemagglutinin) from Phaseolus vulgaris. |journal=Scand. J. Immunol. |volume=23 |issue= 5 |pages= 535-44 |year= 1986 |pmid= 3085210 |doi= }}
*{{cite journal | author=Sewell WA, Brown MH, Dunne J, ''et al.'' |title=Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 22 |pages= 8718-22 |year= 1986 |pmid= 3490670 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDX2... {November 14, 2007 5:37:07 PM PST}
- SEARCH REDIRECT: Control Box Found: CDX2 {November 14, 2007 5:37:47 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:37:49 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:37:49 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:37:49 PM PST}
- UPDATED: Updated protein page: CDX2 {November 14, 2007 5:37:56 PM PST}
- INFO: Beginning work on CPB2... {November 14, 2007 5:37:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:38:26 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Carboxypeptidase B2 (plasma)
| HGNCid = 2300
| Symbol = CPB2
| AltSymbols =; PCPB; CPU; TAFI
| OMIM = 603101
| ECnumber =
| Homologene = 55610
| MGIid = 1891837
| GeneAtlas_image1 = PBB_GE_CPB2_206651_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004182 |text = carboxypeptidase A activity}} {{GNF_GO|id=GO:0004184 |text = lysine carboxypeptidase activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1361
| Hs_Ensembl = ENSG00000080618
| Hs_RefseqProtein = NP_001863
| Hs_RefseqmRNA = NM_001872
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 45525323
| Hs_GenLoc_end = 45577169
| Hs_Uniprot = Q96IY4
| Mm_EntrezGene = 56373
| Mm_Ensembl = ENSMUSG00000021999
| Mm_RefseqmRNA = NM_019775
| Mm_RefseqProtein = NP_062749
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 73976442
| Mm_GenLoc_end = 74017703
| Mm_Uniprot = Q9JHH6
}}
}}
'''Carboxypeptidase B2 (plasma)''', also known as '''CPB2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Available sequence data analyses indicate splice variants that encode different isoforms.<ref>{{cite web | title = Entrez Gene: CPB2 carboxypeptidase B2 (plasma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1361| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bouma BN, Mosnier LO |title=Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis. |journal=Pathophysiol. Haemost. Thromb. |volume=33 |issue= 5-6 |pages= 375-81 |year= 2005 |pmid= 15692247 |doi= 10.1159/000083832 }}
*{{cite journal | author=Marinkovic DV, Marinkovic JN, Erdös EG, Robinson CJ |title=Purification of carboxypeptidase B from human pancreas. |journal=Biochem. J. |volume=163 |issue= 2 |pages= 253-60 |year= 1977 |pmid= 17398 |doi= }}
*{{cite journal | author=Tsai SP, Drayna D |title=The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome 13. |journal=Genomics |volume=14 |issue= 2 |pages= 549-50 |year= 1992 |pmid= 1427879 |doi= }}
*{{cite journal | author=Eaton DL, Malloy BE, Tsai SP, ''et al.'' |title=Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. |journal=J. Biol. Chem. |volume=266 |issue= 32 |pages= 21833-8 |year= 1991 |pmid= 1939207 |doi= }}
*{{cite journal | author=Pascual R, Burgos FJ, Salva M, ''et al.'' |title=Purification and properties of five different forms of human procarboxypeptidases. |journal=Eur. J. Biochem. |volume=179 |issue= 3 |pages= 609-16 |year= 1989 |pmid= 2920728 |doi= }}
*{{cite journal | author=Valnickova Z, Thogersen IB, Christensen S, ''et al.'' |title=Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein. |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 12937-43 |year= 1996 |pmid= 8662763 |doi= }}
*{{cite journal | author=Bajzar L, Morser J, Nesheim M |title=TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16603-8 |year= 1996 |pmid= 8663147 |doi= }}
*{{cite journal | author=Vanhoof G, Wauters J, Schatteman K, ''et al.'' |title=The gene for human carboxypeptidase U (CPU)--a proposed novel regulator of plasminogen activation--maps to 13q14.11. |journal=Genomics |volume=38 |issue= 3 |pages= 454-5 |year= 1997 |pmid= 8975730 |doi= 10.1006/geno.1996.0656 }}
*{{cite journal | author=Zhao L, Morser J, Bajzar L, ''et al.'' |title=Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms. |journal=Thromb. Haemost. |volume=80 |issue= 6 |pages= 949-55 |year= 1999 |pmid= 9869166 |doi= }}
*{{cite journal | author=Boffa MB, Reid TS, Joo E, ''et al.'' |title=Characterization of the gene encoding human TAFI (thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidase B). |journal=Biochemistry |volume=38 |issue= 20 |pages= 6547-58 |year= 1999 |pmid= 10350473 |doi= 10.1021/bi990229v }}
*{{cite journal | author=Matsumoto A, Itoh K, Matsumoto R |title=A novel carboxypeptidase B that processes native beta-amyloid precursor protein is present in human hippocampus. |journal=Eur. J. Neurosci. |volume=12 |issue= 1 |pages= 227-38 |year= 2000 |pmid= 10651877 |doi= }}
*{{cite journal | author=Marx PF, Hackeng TM, Dawson PE, ''et al.'' |title=Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12410-5 |year= 2000 |pmid= 10777524 |doi= }}
*{{cite journal | author=Mosnier LO, Lisman T, van den Berg HM, ''et al.'' |title=The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1035-9 |year= 2002 |pmid= 11686321 |doi= }}
*{{cite journal | author=Mosnier LO, Meijers JC, Bouma BN |title=The role of protein S in the activation of thrombin activatable fibrinolysis inhibitor (TAFI) and regulation of fibrinolysis. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1040-6 |year= 2002 |pmid= 11686322 |doi= }}
*{{cite journal | author=Mosnier LO, Elisen MG, Bouma BN, Meijers JC |title=Protein C inhibitor regulates the thrombin-thrombomodulin complex in the up- and down regulation of TAFI activation. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1057-64 |year= 2002 |pmid= 11686324 |doi= }}
*{{cite journal | author=Morange PE, Aillaud MF, Nicaud V, ''et al.'' |title=Ala147Thr and C+1542G polymorphisms in the TAFI gene are not asssociated with a higher risk of venous thrombosis in FV Leiden carriers. |journal=Thromb. Haemost. |volume=86 |issue= 6 |pages= 1583-4 |year= 2002 |pmid= 11776333 |doi= }}
*{{cite journal | author=Schneider M, Nagashima M, Knappe S, ''et al.'' |title=Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 9944-51 |year= 2002 |pmid= 11786552 |doi= 10.1074/jbc.M111685200 }}
*{{cite journal | author=Koschinsky ML, Boffa MB, Nesheim ME, ''et al.'' |title=Association of a single nucleotide polymorphism in CPB2 encoding the thrombin-activable fibrinolysis inhibitor (TAF1) with blood pressure. |journal=Clin. Genet. |volume=60 |issue= 5 |pages= 345-9 |year= 2002 |pmid= 11903334 |doi= }}
*{{cite journal | author=Yano Y, Gabazza EC, Hori Y, ''et al.'' |title=Association between plasma thrombin-activatable fibrinolysis inhibitor levels and activated protein C in normotensive type 2 diabetic patients. |journal=Diabetes Care |volume=25 |issue= 7 |pages= 1245-6 |year= 2002 |pmid= 12087030 |doi= }}
*{{cite journal | author=Antovic JP, Blombäck M |title=Thrombin-activatable fibrinolysis inhibitor antigen and TAFI activity in patients with APC resistance caused by factor V Leiden mutation. |journal=Thromb. Res. |volume=106 |issue= 1 |pages= 59-62 |year= 2003 |pmid= 12165290 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSF3... {November 14, 2007 5:38:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:39:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CSF3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cd9.
| PDB = {{PDB2|1cd9}}, {{PDB2|1gnc}}, {{PDB2|1pgr}}, {{PDB2|1rhg}}, {{PDB2|2d9q}}
| Name = Colony stimulating factor 3 (granulocyte)
| HGNCid = 2438
| Symbol = CSF3
| AltSymbols =; G-CSF; GCSF; MGC45931
| OMIM = 138970
| ECnumber =
| Homologene = 7677
| MGIid = 1339751
| GeneAtlas_image1 = PBB_GE_CSF3_207442_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005130 |text = granulocyte colony-stimulating factor receptor binding}} {{GNF_GO|id=GO:0005138 |text = interleukin-6 receptor binding}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006953 |text = acute-phase response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}} {{GNF_GO|id=GO:0030851 |text = granulocyte differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1440
| Hs_Ensembl = ENSG00000108342
| Hs_RefseqProtein = NP_000750
| Hs_RefseqmRNA = NM_000759
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 35425214
| Hs_GenLoc_end = 35427592
| Hs_Uniprot = P09919
| Mm_EntrezGene = 12985
| Mm_Ensembl = ENSMUSG00000038067
| Mm_RefseqmRNA = NM_009971
| Mm_RefseqProtein = NP_034101
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 98517403
| Mm_GenLoc_end = 98519719
| Mm_Uniprot = Q0VB73
}}
}}
'''Colony stimulating factor 3 (granulocyte)''', also known as '''CSF3''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: CSF3 colony stimulating factor 3 (granulocyte)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1440| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Duarte RF, Franf DA |title=The synergy between stem cell factor (SCF) and granulocyte colony-stimulating factor (G-CSF): molecular basis and clinical relevance. |journal=Leuk. Lymphoma |volume=43 |issue= 6 |pages= 1179-87 |year= 2003 |pmid= 12152985 |doi= }}
*{{cite journal | author=Mroczko B, Szmitkowski M |title=Hematopoietic cytokines as tumor markers. |journal=Clin. Chem. Lab. Med. |volume=42 |issue= 12 |pages= 1347-54 |year= 2005 |pmid= 15576295 |doi= 10.1515/CCLM.2004.253 }}
*{{cite journal | author=Sallerfors B, Olofsson T |title=Granulocyte-macrophage colony-stimulating factor (GM-CSF) and granulocyte colony-stimulating factor (G-CSF) secretion by adherent monocytes measured by quantitative immunoassays. |journal=Eur. J. Haematol. |volume=49 |issue= 4 |pages= 199-207 |year= 1993 |pmid= 1281454 |doi= }}
*{{cite journal | author=Zink T, Ross A, Ambrosius D, ''et al.'' |title=Secondary structure of human granulocyte colony-stimulating factor derived from NMR spectroscopy. |journal=FEBS Lett. |volume=314 |issue= 3 |pages= 435-9 |year= 1993 |pmid= 1281794 |doi= }}
*{{cite journal | author=Kubota N, Orita T, Hattori K, ''et al.'' |title=Structural characterization of natural and recombinant human granulocyte colony-stimulating factors. |journal=J. Biochem. |volume=107 |issue= 3 |pages= 486-92 |year= 1990 |pmid= 1692828 |doi= }}
*{{cite journal | author=Souza LM, Boone TC, Gabrilove J, ''et al.'' |title=Recombinant human granulocyte colony-stimulating factor: effects on normal and leukemic myeloid cells. |journal=Science |volume=232 |issue= 4746 |pages= 61-5 |year= 1986 |pmid= 2420009 |doi= }}
*{{cite journal | author=Nagata S, Tsuchiya M, Asano S, ''et al.'' |title=The chromosomal gene structure and two mRNAs for human granulocyte colony-stimulating factor. |journal=EMBO J. |volume=5 |issue= 3 |pages= 575-81 |year= 1986 |pmid= 2423327 |doi= }}
*{{cite journal | author=Simmers RN, Smith J, Shannon MF, ''et al.'' |title=Localization of the human G-CSF gene to the region of a breakpoint in the translocation typical of acute promyelocytic leukemia. |journal=Hum. Genet. |volume=78 |issue= 2 |pages= 134-6 |year= 1988 |pmid= 2448221 |doi= }}
*{{cite journal | author=Tweardy DJ, Cannizzaro LA, Palumbo AP, ''et al.'' |title=Molecular cloning and characterization of a cDNA for human granulocyte colony-stimulating factor (G-CSF) from a glioblastoma multiforme cell line and localization of the G-CSF gene to chromosome band 17q21. |journal=Oncogene Res. |volume=1 |issue= 3 |pages= 209-20 |year= 1988 |pmid= 2453015 |doi= }}
*{{cite journal | author=Tsuchiya M, Nomura H, Asano S, ''et al.'' |title=Characterization of recombinant human granulocyte-colony-stimulating factor produced in mouse cells. |journal=EMBO J. |volume=6 |issue= 3 |pages= 611-6 |year= 1987 |pmid= 3034599 |doi= }}
*{{cite journal | author=Nagata S, Tsuchiya M, Asano S, ''et al.'' |title=Molecular cloning and expression of cDNA for human granulocyte colony-stimulating factor. |journal=Nature |volume=319 |issue= 6052 |pages= 415-8 |year= 1986 |pmid= 3484805 |doi= 10.1038/319415a0 }}
*{{cite journal | author=Devlin JJ, Devlin PE, Myambo K, ''et al.'' |title=Expression of granulocyte colony-stimulating factor by human cell lines. |journal=J. Leukoc. Biol. |volume=41 |issue= 4 |pages= 302-6 |year= 1987 |pmid= 3494801 |doi= }}
*{{cite journal | author=Kanda N, Fukushige S, Murotsu T, ''et al.'' |title=Human gene coding for granulocyte-colony stimulating factor is assigned to the q21-q22 region of chromosome 17. |journal=Somat. Cell Mol. Genet. |volume=13 |issue= 6 |pages= 679-84 |year= 1987 |pmid= 3499671 |doi= }}
*{{cite journal | author=Le Beau MM, Lemons RS, Carrino JJ, ''et al.'' |title=Chromosomal localization of the human G-CSF gene to 17q11 proximal to the breakpoint of the t(15;17) in acute promyelocytic leukemia. |journal=Leukemia |volume=1 |issue= 12 |pages= 795-9 |year= 1988 |pmid= 3501046 |doi= }}
*{{cite journal | author=Zink T, Ross A, Lüers K, ''et al.'' |title=Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein. |journal=Biochemistry |volume=33 |issue= 28 |pages= 8453-63 |year= 1994 |pmid= 7518249 |doi= }}
*{{cite journal | author=Corcione A, Baldi L, Zupo S, ''et al.'' |title=Spontaneous production of granulocyte colony-stimulating factor in vitro by human B-lineage lymphocytes is a distinctive marker of germinal center cells. |journal=J. Immunol. |volume=153 |issue= 7 |pages= 2868-77 |year= 1994 |pmid= 7522243 |doi= }}
*{{cite journal | author=Watari K, Ozawa K, Tajika K, ''et al.'' |title=Production of human granulocyte colony stimulating factor by various kinds of stromal cells in vitro detected by enzyme immunoassay and in situ hybridization. |journal=Stem Cells |volume=12 |issue= 4 |pages= 416-23 |year= 1994 |pmid= 7524894 |doi= }}
*{{cite journal | author=Hill CP, Osslund TD, Eisenberg D |title=The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 11 |pages= 5167-71 |year= 1993 |pmid= 7685117 |doi= }}
*{{cite journal | author=Haniu M, Horan T, Arakawa T, ''et al.'' |title=Extracellular domain of granulocyte-colony stimulating factor receptor. Interaction with its ligand and identification of a domain in close proximity of ligand-binding region. |journal=Arch. Biochem. Biophys. |volume=324 |issue= 2 |pages= 344-56 |year= 1996 |pmid= 8554326 |doi= 10.1006/abbi.1995.0047 }}
*{{cite journal | author=McCracken S, Layton JE, Shorter SC, ''et al.'' |title=Expression of granulocyte-colony stimulating factor and its receptor is regulated during the development of the human placenta. |journal=J. Endocrinol. |volume=149 |issue= 2 |pages= 249-58 |year= 1996 |pmid= 8708536 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTBP1... {November 14, 2007 5:39:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:39:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CTBP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hku.
| PDB = {{PDB2|1hku}}, {{PDB2|1hl3}}, {{PDB2|1mx3}}, {{PDB2|2hu2}}
| Name = C-terminal binding protein 1
| HGNCid = 2494
| Symbol = CTBP1
| AltSymbols =; BARS; MGC104684
| OMIM = 602618
| ECnumber =
| Homologene = 1015
| MGIid = 1201685
| GeneAtlas_image1 = PBB_GE_CTBP1_203392_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CTBP1_212863_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CTBP1_213980_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016616 |text = oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor}} {{GNF_GO|id=GO:0051287 |text = NAD binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006564 |text = L-serine biosynthetic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0019079 |text = viral genome replication}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1487
| Hs_Ensembl = ENSG00000159692
| Hs_RefseqProtein = NP_001012632
| Hs_RefseqmRNA = NM_001012614
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 1195228
| Hs_GenLoc_end = 1232925
| Hs_Uniprot = Q13363
| Mm_EntrezGene = 13016
| Mm_Ensembl = ENSMUSG00000037373
| Mm_RefseqmRNA = XM_990134
| Mm_RefseqProtein = XP_995228
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 33564581
| Mm_GenLoc_end = 33591839
| Mm_Uniprot = Q3TAT1
}}
}}
'''C-terminal binding protein 1''', also known as '''CTBP1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein that binds to the C-terminus of adenovirus E1A proteins. This phosphoprotein is a transcriptional repressor and may play a role during cellular proliferation. This protein and the product of a second closely related gene, CTBP2, can dimerize. Both proteins can also interact with a polycomb group protein complex which participates in regulation of gene expression during development. Alternative splicing of transcripts from this gene results in multiple transcript variants.<ref>{{cite web | title = Entrez Gene: CTBP1 C-terminal binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1487| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chinnadurai G |title=CtBP, an unconventional transcriptional corepressor in development and oncogenesis. |journal=Mol. Cell |volume=9 |issue= 2 |pages= 213-24 |year= 2002 |pmid= 11864595 |doi= }}
*{{cite journal | author=Schaeper U, Boyd JM, Verma S, ''et al.'' |title=Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 23 |pages= 10467-71 |year= 1995 |pmid= 7479821 |doi= }}
*{{cite journal | author=Boyd JM, Subramanian T, Schaeper U, ''et al.'' |title=A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasis. |journal=EMBO J. |volume=12 |issue= 2 |pages= 469-78 |year= 1993 |pmid= 8440238 |doi= }}
*{{cite journal | author=Katsanis N, Fisher EM |title=A novel C-terminal binding protein (CTBP2) is closely related to CTBP1, an adenovirus E1A-binding protein, and maps to human chromosome 21q21.3. |journal=Genomics |volume=47 |issue= 2 |pages= 294-9 |year= 1998 |pmid= 9479502 |doi= 10.1006/geno.1997.5115 }}
*{{cite journal | author=Schaeper U, Subramanian T, Lim L, ''et al.'' |title=Interaction between a cellular protein that binds to the C-terminal region of adenovirus E1A (CtBP) and a novel cellular protein is disrupted by E1A through a conserved PLDLS motif. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 8549-52 |year= 1998 |pmid= 9535825 |doi= }}
*{{cite journal | author=Sundqvist A, Sollerbrant K, Svensson C |title=The carboxy-terminal region of adenovirus E1A activates transcription through targeting of a C-terminal binding protein-histone deacetylase complex. |journal=FEBS Lett. |volume=429 |issue= 2 |pages= 183-8 |year= 1998 |pmid= 9650586 |doi= }}
*{{cite journal | author=Fuks F, Milner J, Kouzarides T |title=BRCA2 associates with acetyltransferase activity when bound to P/CAF. |journal=Oncogene |volume=17 |issue= 19 |pages= 2531-4 |year= 1998 |pmid= 9824164 |doi= 10.1038/sj.onc.1202475 }}
*{{cite journal | author=Sewalt RG, Gunster MJ, van der Vlag J, ''et al.'' |title=C-Terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate Polycomb proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 1 |pages= 777-87 |year= 1999 |pmid= 9858600 |doi= }}
*{{cite journal | author=Li S, Chen PL, Subramanian T, ''et al.'' |title=Binding of CtIP to the BRCT repeats of BRCA1 involved in the transcription regulation of p21 is disrupted upon DNA damage. |journal=J. Biol. Chem. |volume=274 |issue= 16 |pages= 11334-8 |year= 1999 |pmid= 10196224 |doi= }}
*{{cite journal | author=Postigo AA, Dean DC |title=ZEB represses transcription through interaction with the corepressor CtBP. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 12 |pages= 6683-8 |year= 1999 |pmid= 10359772 |doi= }}
*{{cite journal | author=Criqui-Filipe P, Ducret C, Maira SM, Wasylyk B |title=Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation. |journal=EMBO J. |volume=18 |issue= 12 |pages= 3392-403 |year= 1999 |pmid= 10369679 |doi= 10.1093/emboj/18.12.3392 }}
*{{cite journal | author=Holmes M, Turner J, Fox A, ''et al.'' |title=hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2 and modulates GATA-mediated activation. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23491-8 |year= 1999 |pmid= 10438528 |doi= }}
*{{cite journal | author=Furusawa T, Moribe H, Kondoh H, Higashi Y |title=Identification of CtBP1 and CtBP2 as corepressors of zinc finger-homeodomain factor deltaEF1. |journal=Mol. Cell. Biol. |volume=19 |issue= 12 |pages= 8581-90 |year= 2000 |pmid= 10567582 |doi= }}
*{{cite journal | author=Yu X, Baer R |title=Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18541-9 |year= 2000 |pmid= 10764811 |doi= 10.1074/jbc.M909494199 }}
*{{cite journal | author=Koipally J, Georgopoulos K |title=Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19594-602 |year= 2000 |pmid= 10766745 |doi= 10.1074/jbc.M000254200 }}
*{{cite journal | author=Melhuish TA, Wotton D |title=The interaction of the carboxyl terminus-binding protein with the Smad corepressor TGIF is disrupted by a holoprosencephaly mutation in TGIF. |journal=J. Biol. Chem. |volume=275 |issue= 50 |pages= 39762-6 |year= 2001 |pmid= 10995736 |doi= 10.1074/jbc.C000416200 }}
*{{cite journal | author=Zhang CL, McKinsey TA, Lu JR, Olson EN |title=Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 35-9 |year= 2001 |pmid= 11022042 |doi= 10.1074/jbc.M007364200 }}
*{{cite journal | author=Izutsu K, Kurokawa M, Imai Y, ''et al.'' |title=The corepressor CtBP interacts with Evi-1 to repress transforming growth factor beta signaling. |journal=Blood |volume=97 |issue= 9 |pages= 2815-22 |year= 2001 |pmid= 11313276 |doi= }}
*{{cite journal | author=Palmer S, Brouillet JP, Kilbey A, ''et al.'' |title=Evi-1 transforming and repressor activities are mediated by CtBP co-repressor proteins. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 25834-40 |year= 2001 |pmid= 11328817 |doi= 10.1074/jbc.M102343200 }}
*{{cite journal | author=Schuierer M, Hilger-Eversheim K, Dobner T, ''et al.'' |title=Induction of AP-2alpha expression by adenoviral infection involves inactivation of the AP-2rep transcriptional corepressor CtBP1. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 27944-9 |year= 2001 |pmid= 11373277 |doi= 10.1074/jbc.M100070200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP2A6... {November 14, 2007 5:39:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:40:28 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CYP2A6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z10.
| PDB = {{PDB2|1z10}}, {{PDB2|1z11}}, {{PDB2|2fdu}}, {{PDB2|2fdv}}, {{PDB2|2fdw}}, {{PDB2|2fdy}}, {{PDB2|2p85}}
| Name = Cytochrome P450, family 2, subfamily A, polypeptide 6
| HGNCid = 2610
| Symbol = CYP2A6
| AltSymbols =; CYP2A; P450C2A; P450PB; CPA6; CYP2A3; CPA7; CPAD; CYPIIA7; P450-IIA4
| OMIM = 122720
| ECnumber =
| Homologene = 86656
| MGIid =
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008389 |text = coumarin 7-hydroxylase activity}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050381 |text = unspecific monooxygenase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1548
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000753
| Hs_RefseqmRNA = NM_000762
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cytochrome P450, family 2, subfamily A, polypeptide 6''', also known as '''CYP2A6''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene, CYP2A6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and its expression is induced by phenobarbital. The enzyme is known to hydroxylate coumarin, and also metabolizes nicotine, aflatoxin B1, nitrosamines, and some pharmaceuticals. Individuals with certain allelic variants are said to have a poor metabolizer phenotype, meaning they do not efficiently metabolize coumarin or nicotine. This gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. The gene was formerly referred to as CYP2A3; however, it has been renamed CYP2A6.<ref>{{cite web | title = Entrez Gene: CYP2A6 cytochrome P450, family 2, subfamily A, polypeptide 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1548| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fernandez-Salguero P, Gonzalez FJ |title=The CYP2A gene subfamily: species differences, regulation, catalytic activities and role in chemical carcinogenesis. |journal=Pharmacogenetics |volume=5 Spec No |issue= |pages= S123-8 |year= 1995 |pmid= 7581481 |doi= }}
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Pelkonen O, Rautio A, Raunio H, Pasanen M |title=CYP2A6: a human coumarin 7-hydroxylase. |journal=Toxicology |volume=144 |issue= 1-3 |pages= 139-47 |year= 2000 |pmid= 10781881 |doi= }}
*{{cite journal | author=Tyndale RF, Sellers EM |title=Genetic variation in CYP2A6-mediated nicotine metabolism alters smoking behavior. |journal=Therapeutic drug monitoring |volume=24 |issue= 1 |pages= 163-71 |year= 2002 |pmid= 11805739 |doi= }}
*{{cite journal | author=Xu C, Goodz S, Sellers EM, Tyndale RF |title=CYP2A6 genetic variation and potential consequences. |journal=Adv. Drug Deliv. Rev. |volume=54 |issue= 10 |pages= 1245-56 |year= 2003 |pmid= 12406643 |doi= }}
*{{cite journal | author=Kamataki T, Fujieda M, Kiyotani K, ''et al.'' |title=Genetic polymorphism of CYP2A6 as one of the potential determinants of tobacco-related cancer risk. |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue= 1 |pages= 306-10 |year= 2005 |pmid= 16176798 |doi= 10.1016/j.bbrc.2005.08.268 }}
*{{cite journal | author=Maurice M, Emiliani S, Dalet-Beluche I, ''et al.'' |title=Isolation and characterization of a cytochrome P450 of the IIA subfamily from human liver microsomes. |journal=Eur. J. Biochem. |volume=200 |issue= 2 |pages= 511-7 |year= 1991 |pmid= 1889415 |doi= }}
*{{cite journal | author=Yun CH, Shimada T, Guengerich FP |title=Purification and characterization of human liver microsomal cytochrome P-450 2A6. |journal=Mol. Pharmacol. |volume=40 |issue= 5 |pages= 679-85 |year= 1991 |pmid= 1944238 |doi= }}
*{{cite journal | author=Yamano S, Tatsuno J, Gonzalez FJ |title=The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. |journal=Biochemistry |volume=29 |issue= 5 |pages= 1322-9 |year= 1990 |pmid= 2322567 |doi= }}
*{{cite journal | author=Miles JS, Bickmore W, Brook JD, ''et al.'' |title=Close linkage of the human cytochrome P450IIA and P450IIB gene subfamilies: implications for the assignment of substrate specificity. |journal=Nucleic Acids Res. |volume=17 |issue= 8 |pages= 2907-17 |year= 1989 |pmid= 2726448 |doi= }}
*{{cite journal | author=Yamano S, Nagata K, Yamazoe Y, ''et al.'' |title=cDNA and deduced amino acid sequences of human P450 IIA3 (CYP2A3). |journal=Nucleic Acids Res. |volume=17 |issue= 12 |pages= 4888 |year= 1989 |pmid= 2748347 |doi= }}
*{{cite journal | author=Phillips IR, Shephard EA, Ashworth A, Rabin BR |title=Isolation and sequence of a human cytochrome P-450 cDNA clone. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 4 |pages= 983-7 |year= 1985 |pmid= 3856261 |doi= }}
*{{cite journal | author=Wainwright BJ, Watson EK, Shephard EA, Phillips IR |title=RFLP for a human cytochrome P-450 gene at 19q13.1-qter (HGM8 provisional designation CYPI). |journal=Nucleic Acids Res. |volume=13 |issue= 12 |pages= 4610 |year= 1985 |pmid= 4011450 |doi= }}
*{{cite journal | author=Fernandez-Salguero P, Hoffman SM, Cholerton S, ''et al.'' |title=A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. |journal=Am. J. Hum. Genet. |volume=57 |issue= 3 |pages= 651-60 |year= 1995 |pmid= 7668294 |doi= }}
*{{cite journal | author=Ding S, Lake BG, Friedberg T, Wolf CR |title=Expression and alternative splicing of the cytochrome P-450 CYP2A7. |journal=Biochem. J. |volume=306 ( Pt 1) |issue= |pages= 161-6 |year= 1995 |pmid= 7864805 |doi= }}
*{{cite journal | author=Hoffman SM, Fernandez-Salguero P, Gonzalez FJ, Mohrenweiser HW |title=Organization and evolution of the cytochrome P450 CYP2A-2B-2F subfamily gene cluster on human chromosome 19. |journal=J. Mol. Evol. |volume=41 |issue= 6 |pages= 894-900 |year= 1996 |pmid= 8587134 |doi= }}
*{{cite journal | author=Hadidi H, Zahlsen K, Idle JR, Cholerton S |title=A single amino acid substitution (Leu160His) in cytochrome P450 CYP2A6 causes switching from 7-hydroxylation to 3-hydroxylation of coumarin. |journal=Food Chem. Toxicol. |volume=35 |issue= 9 |pages= 903-7 |year= 1998 |pmid= 9409631 |doi= }}
*{{cite journal | author=Oscarson M, Gullstén H, Rautio A, ''et al.'' |title=Genotyping of human cytochrome P450 2A6 (CYP2A6), a nicotine C-oxidase. |journal=FEBS Lett. |volume=438 |issue= 3 |pages= 201-5 |year= 1998 |pmid= 9827545 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ELAVL1... {November 14, 2007 5:41:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:42:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ELAV (embryonic lethal, abnormal vision, Drosophila)-like 1 (Hu antigen R)
| HGNCid = 3312
| Symbol = ELAVL1
| AltSymbols =; ELAV1; HUR; Hua; MelG
| OMIM = 603466
| ECnumber =
| Homologene = 20367
| MGIid = 1100851
| GeneAtlas_image1 = PBB_GE_ELAVL1_201726_at_tn.png
| GeneAtlas_image2 = PBB_GE_ELAVL1_201727_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003730 |text = mRNA 3'-UTR binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006401 |text = RNA catabolic process}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0048255 |text = mRNA stabilization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1994
| Hs_Ensembl = ENSG00000066044
| Hs_RefseqProtein = NP_001410
| Hs_RefseqmRNA = NM_001419
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 7933159
| Hs_GenLoc_end = 8415925
| Hs_Uniprot = Q15717
| Mm_EntrezGene = 15568
| Mm_Ensembl = ENSMUSG00000040028
| Mm_RefseqmRNA = NM_010485
| Mm_RefseqProtein = NP_034615
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 4288343
| Mm_GenLoc_end = 4325086
| Mm_Uniprot = Q3TT05
}}
}}
'''ELAV (embryonic lethal, abnormal vision, Drosophila)-like 1 (Hu antigen R)''', also known as '''ELAVL1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the ELAVL protein family. This encoded protein contains 3 RNA-binding domains and binds cis-acting AU-rich elements. It destabilizes mRNAs and thereby regulates gene expression.<ref>{{cite web | title = Entrez Gene: ELAVL1 ELAV (embryonic lethal, abnormal vision, Drosophila)-like 1 (Hu antigen R)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1994| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Abdelmohsen K, Lal A, Kim HH, Gorospe M |title=Posttranscriptional orchestration of an anti-apoptotic program by HuR. |journal=Cell Cycle |volume=6 |issue= 11 |pages= 1288-92 |year= 2007 |pmid= 17534146 |doi= }}
*{{cite journal | author=Ma WJ, Cheng S, Campbell C, ''et al.'' |title=Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8144-51 |year= 1996 |pmid= 8626503 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Ma WJ, Furneaux H |title=Localization of the human HuR gene to chromosome 19p13.2. |journal=Hum. Genet. |volume=99 |issue= 1 |pages= 32-3 |year= 1997 |pmid= 9003489 |doi= }}
*{{cite journal | author=Sakai K, Kitagawa Y, Hirose G |title=Analysis of the RNA recognition motifs of human neuronal ELAV-like proteins in binding to a cytokine mRNA. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 2 |pages= 263-8 |year= 1999 |pmid= 10079173 |doi= 10.1006/bbrc.1999.0282 }}
*{{cite journal | author=Wang W, Furneaux H, Cheng H, ''et al.'' |title=HuR regulates p21 mRNA stabilization by UV light. |journal=Mol. Cell. Biol. |volume=20 |issue= 3 |pages= 760-9 |year= 2000 |pmid= 10629032 |doi= }}
*{{cite journal | author=Blaxall BC, Pellett AC, Wu SC, ''et al.'' |title=Purification and characterization of beta-adrenergic receptor mRNA-binding proteins. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4290-7 |year= 2000 |pmid= 10660597 |doi= }}
*{{cite journal | author=Park S, Myszka DG, Yu M, ''et al.'' |title=HuD RNA recognition motifs play distinct roles in the formation of a stable complex with AU-rich RNA. |journal=Mol. Cell. Biol. |volume=20 |issue= 13 |pages= 4765-72 |year= 2000 |pmid= 10848602 |doi= }}
*{{cite journal | author=Spångberg K, Wiklund L, Schwartz S |title=HuR, a protein implicated in oncogene and growth factor mRNA decay, binds to the 3' ends of hepatitis C virus RNA of both polarities. |journal=Virology |volume=274 |issue= 2 |pages= 378-90 |year= 2000 |pmid= 10964780 |doi= 10.1006/viro.2000.0461 }}
*{{cite journal | author=Brennan CM, Gallouzi IE, Steitz JA |title=Protein ligands to HuR modulate its interaction with target mRNAs in vivo. |journal=J. Cell Biol. |volume=151 |issue= 1 |pages= 1-14 |year= 2000 |pmid= 11018049 |doi= }}
*{{cite journal | author=Gallouzi IE, Brennan CM, Steitz JA |title=Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock. |journal=RNA |volume=7 |issue= 9 |pages= 1348-61 |year= 2001 |pmid= 11565755 |doi= }}
*{{cite journal | author=Gallouzi IE, Steitz JA |title=Delineation of mRNA export pathways by the use of cell-permeable peptides. |journal=Science |volume=294 |issue= 5548 |pages= 1895-901 |year= 2001 |pmid= 11729309 |doi= 10.1126/science.1064693 }}
*{{cite journal | author=Goldberg-Cohen I, Furneauxb H, Levy AP |title=A 40-bp RNA element that mediates stabilization of vascular endothelial growth factor mRNA by HuR. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13635-40 |year= 2002 |pmid= 11834731 |doi= 10.1074/jbc.M108703200 }}
*{{cite journal | author=Wang W, Fan J, Yang X, ''et al.'' |title=AMP-activated kinase regulates cytoplasmic HuR. |journal=Mol. Cell. Biol. |volume=22 |issue= 10 |pages= 3425-36 |year= 2002 |pmid= 11971974 |doi= }}
*{{cite journal | author=Yeap BB, Voon DC, Vivian JP, ''et al.'' |title=Novel binding of HuR and poly(C)-binding protein to a conserved UC-rich motif within the 3'-untranslated region of the androgen receptor messenger RNA. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27183-92 |year= 2002 |pmid= 12011088 |doi= 10.1074/jbc.M202883200 }}
*{{cite journal | author=Li H, Park S, Kilburn B, ''et al.'' |title=Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 44623-30 |year= 2003 |pmid= 12237300 |doi= 10.1074/jbc.M206187200 }}
*{{cite journal | author=Chen CY, Xu N, Shyu AB |title=Highly selective actions of HuR in antagonizing AU-rich element-mediated mRNA destabilization. |journal=Mol. Cell. Biol. |volume=22 |issue= 20 |pages= 7268-78 |year= 2002 |pmid= 12242302 |doi= }}
*{{cite journal | author=Giles KM, Daly JM, Beveridge DJ, ''et al.'' |title=The 3'-untranslated region of p21WAF1 mRNA is a composite cis-acting sequence bound by RNA-binding proteins from breast cancer cells, including HuR and poly(C)-binding protein. |journal=J. Biol. Chem. |volume=278 |issue= 5 |pages= 2937-46 |year= 2003 |pmid= 12431987 |doi= 10.1074/jbc.M208439200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Wang W, Yang X, López de Silanes I, ''et al.'' |title=Increased AMP:ATP ratio and AMP-activated protein kinase activity during cellular senescence linked to reduced HuR function. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 27016-23 |year= 2003 |pmid= 12730239 |doi= 10.1074/jbc.M300318200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGFR4... {November 14, 2007 5:42:12 PM PST}
- SEARCH REDIRECT: Control Box Found: FGFR4 {November 14, 2007 5:43:01 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:43:03 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:43:03 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:43:03 PM PST}
- UPDATED: Updated protein page: FGFR4 {November 14, 2007 5:43:10 PM PST}
- INFO: Beginning work on FKBP1A... {November 14, 2007 5:43:10 PM PST}
- SEARCH REDIRECT: Control Box Found: FKBP1A {November 14, 2007 5:44:00 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:44:01 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:44:01 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:44:01 PM PST}
- UPDATED: Updated protein page: FKBP1A {November 14, 2007 5:44:08 PM PST}
- INFO: Beginning work on HBE1... {November 14, 2007 5:44:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:44:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HBE1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a9w.
| PDB = {{PDB2|1a9w}}
| Name = Hemoglobin, epsilon 1
| HGNCid = 4830
| Symbol = HBE1
| AltSymbols =; HBE
| OMIM = 142100
| ECnumber =
| Homologene = 74550
| MGIid = 96027
| Function = {{GNF_GO|id=GO:0005344 |text = oxygen transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005833 |text = hemoglobin complex}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0015671 |text = oxygen transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3046
| Hs_Ensembl =
| Hs_RefseqProtein = NP_005321
| Hs_RefseqmRNA = NM_005330
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 15135
| Mm_Ensembl = ENSMUSG00000052187
| Mm_RefseqmRNA = XM_973830
| Mm_RefseqProtein = XP_978924
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 103725575
| Mm_GenLoc_end = 103727028
| Mm_Uniprot = Q9CR49
}}
}}
'''Hemoglobin, epsilon 1''', also known as '''HBE1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The epsilon globin gene (HBE) is normally expressed in the embryonic yolk sac: two epsilon chains together with two zeta chains (an alpha-like globin) constitute the embryonic hemoglobin Hb Gower I; two epsilon chains together with two alpha chains form the embryonic Hb Gower II. Both of these embryonic hemoglobins are normally supplanted by fetal, and later, adult hemoglobin. The five beta-like globin genes are found within a 45 kb cluster on chromosome 11 in the following order: 5'-epsilon - G-gamma - A-gamma - delta - beta-3'<ref>{{cite web | title = Entrez Gene: HBE1 hemoglobin, epsilon 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3046| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Higgs DR, Vickers MA, Wilkie AO, ''et al.'' |title=A review of the molecular genetics of the human alpha-globin gene cluster. |journal=Blood |volume=73 |issue= 5 |pages= 1081-104 |year= 1989 |pmid= 2649166 |doi= }}
*{{cite journal | author=Clegg JB |title=Embryonic hemoglobin: sequence of the epsilon and zeta chains. |journal=Tex. Rep. Biol. Med. |volume=40 |issue= |pages= 23-8 |year= 1982 |pmid= 6172865 |doi= }}
*{{cite journal | author=Giardina B, Messana I, Scatena R, Castagnola M |title=The multiple functions of hemoglobin. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=30 |issue= 3 |pages= 165-96 |year= 1995 |pmid= 7555018 |doi= }}
*{{cite journal | author=Chang JC, Kan YW |title=beta 0 thalassemia, a nonsense mutation in man. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=76 |issue= 6 |pages= 2886-9 |year= 1979 |pmid= 88735 |doi= }}
*{{cite journal | author=Proudfoot NJ, Baralle FE |title=Molecular cloning of human epsilon-globin gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=76 |issue= 11 |pages= 5435-9 |year= 1980 |pmid= 160554 |doi= }}
*{{cite journal | author=Proudfoot NJ, Brownlee GG |title=3' non-coding region sequences in eukaryotic messenger RNA. |journal=Nature |volume=263 |issue= 5574 |pages= 211-4 |year= 1976 |pmid= 822353 |doi= }}
*{{cite journal | author=Marotta CA, Forget BG, Cohne-Solal M, ''et al.'' |title=Human beta-globin messenger RNA. I. Nucleotide sequences derived from complementary RNA. |journal=J. Biol. Chem. |volume=252 |issue= 14 |pages= 5019-31 |year= 1977 |pmid= 873928 |doi= }}
*{{cite journal | author=Gelinas R, Endlich B, Pfeiffer C, ''et al.'' |title=G to A substitution in the distal CCAAT box of the A gamma-globin gene in Greek hereditary persistence of fetal haemoglobin. |journal=Nature |volume=313 |issue= 6000 |pages= 323-5 |year= 1985 |pmid= 2578619 |doi= }}
*{{cite journal | author=Collins FS, Metherall JE, Yamakawa M, ''et al.'' |title=A point mutation in the A gamma-globin gene promoter in Greek hereditary persistence of fetal haemoglobin. |journal=Nature |volume=313 |issue= 6000 |pages= 325-6 |year= 1985 |pmid= 2578620 |doi= }}
*{{cite journal | author=Lang KM, Spritz RA |title=Cloning specific complete polyadenylylated 3'-terminal cDNA segments. |journal=Gene |volume=33 |issue= 2 |pages= 191-6 |year= 1985 |pmid= 2581851 |doi= }}
*{{cite journal | author=Ley TJ, Maloney KA, Gordon JI, Schwartz AL |title=Globin gene expression in erythroid human fetal liver cells. |journal=J. Clin. Invest. |volume=83 |issue= 3 |pages= 1032-8 |year= 1989 |pmid= 2921315 |doi= }}
*{{cite journal | author=Chabot B, Black DL, LeMaster DM, Steitz JA |title=The 3' splice site of pre-messenger RNA is recognized by a small nuclear ribonucleoprotein. |journal=Science |volume=230 |issue= 4732 |pages= 1344-9 |year= 1986 |pmid= 2933810 |doi= }}
*{{cite journal | author=Engelke DR, Hoener PA, Collins FS |title=Direct sequencing of enzymatically amplified human genomic DNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 2 |pages= 544-8 |year= 1988 |pmid= 3267215 |doi= }}
*{{cite journal | author=Fei YJ, Stoming TA, Efremov GD, ''et al.'' |title=Beta-thalassemia due to a T----A mutation within the ATA box. |journal=Biochem. Biophys. Res. Commun. |volume=153 |issue= 2 |pages= 741-7 |year= 1988 |pmid= 3382401 |doi= }}
*{{cite journal | author=Prchal JT, Cashman DP, Kan YW |title=Hemoglobin Long Island is caused by a single mutation (adenine to cytosine) resulting in a failure to cleave amino-terminal methionine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 1 |pages= 24-7 |year= 1986 |pmid= 3455755 |doi= }}
*{{cite journal | author=van Santen VL, Spritz RA |title=mRNA precursor splicing in vivo: sequence requirements determined by deletion analysis of an intervening sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 9 |pages= 2885-9 |year= 1985 |pmid= 3857622 |doi= }}
*{{cite journal | author=Ruskin B, Greene JM, Green MR |title=Cryptic branch point activation allows accurate in vitro splicing of human beta-globin intron mutants. |journal=Cell |volume=41 |issue= 3 |pages= 833-44 |year= 1985 |pmid= 3879973 |doi= }}
*{{cite journal | author=Tuan D, Solomon W, Li Q, London IM |title=The "beta-like-globin" gene domain in human erythroid cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 19 |pages= 6384-8 |year= 1985 |pmid= 3879975 |doi= }}
*{{cite journal | author=Orkin SH, Antonarakis SE, Kazazian HH |title=Base substitution at position -88 in a beta-thalassemic globin gene. Further evidence for the role of distal promoter element ACACCC. |journal=J. Biol. Chem. |volume=259 |issue= 14 |pages= 8679-81 |year= 1984 |pmid= 6086605 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HNRPK... {November 14, 2007 5:45:28 PM PST}
- SEARCH REDIRECT: Control Box Found: HNRPK {November 14, 2007 5:46:04 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:46:06 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:46:06 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:46:06 PM PST}
- UPDATED: Updated protein page: HNRPK {November 14, 2007 5:46:14 PM PST}
- INFO: Beginning work on IGF2R... {November 14, 2007 5:46:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:46:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IGF2R_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e6f.
| PDB = {{PDB2|1e6f}}, {{PDB2|1gp0}}, {{PDB2|1gp3}}, {{PDB2|1gqb}}, {{PDB2|2cnj}}
| Name = Insulin-like growth factor 2 receptor
| HGNCid = 5467
| Symbol = IGF2R
| AltSymbols =; CD222; CIMPR; M6P-R; MPRI
| OMIM = 147280
| ECnumber =
| Homologene = 676
| MGIid = 96435
| GeneAtlas_image1 = PBB_GE_IGF2R_201393_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IGF2R_201392_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005010 |text = insulin-like growth factor receptor activity}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005520 |text = insulin-like growth factor binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005641 |text = nuclear envelope lumen}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030140 |text = trans-Golgi network transport vesicle}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3482
| Hs_Ensembl = ENSG00000197081
| Hs_RefseqProtein = NP_000867
| Hs_RefseqmRNA = NM_000876
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 160310121
| Hs_GenLoc_end = 160447573
| Hs_Uniprot = P11717
| Mm_EntrezGene = 16004
| Mm_Ensembl = ENSMUSG00000023830
| Mm_RefseqmRNA = NM_010515
| Mm_RefseqProtein = NP_034645
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 12525771
| Mm_GenLoc_end = 12613022
| Mm_Uniprot = Q7TMR1
}}
}}
'''Insulin-like growth factor 2 receptor''', also known as '''IGF2R''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a receptor for both, insulin-like growth factor 2 (IGF2) and mannose 6-phosphate (M6P). The IGF2 and M6P binding sites are located on different segments of the receptor. This receptor functions in the intracellular trafficking of lysosomal enzymes, the activation of transforming growth factor beta, and the degradation of IGF2. In mice, the homologous gene is expressed only from the maternal chromosome.<ref>{{cite web | title = Entrez Gene: IGF2R insulin-like growth factor 2 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3482| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=O'Dell SD, Day IN |title=Insulin-like growth factor II (IGF-II). |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 7 |pages= 767-71 |year= 1998 |pmid= 9722981 |doi= }}
*{{cite journal | author=Hawkes C, Kar S |title=The insulin-like growth factor-II/mannose-6-phosphate receptor: structure, distribution and function in the central nervous system. |journal=Brain Res. Brain Res. Rev. |volume=44 |issue= 2-3 |pages= 117-40 |year= 2004 |pmid= 15003389 |doi= 10.1016/j.brainresrev.2003.11.002 }}
*{{cite journal | author=Scott CD, Firth SM |title=The role of the M6P/IGF-II receptor in cancer: tumor suppression or garbage disposal? |journal=Horm. Metab. Res. |volume=36 |issue= 5 |pages= 261-71 |year= 2005 |pmid= 15156403 |doi= 10.1055/s-2004-814477 }}
*{{cite journal | author=Antoniades HN, Galanopoulos T, Neville-Golden J, Maxwell M |title=Expression of insulin-like growth factors I and II and their receptor mRNAs in primary human astrocytomas and meningiomas; in vivo studies using in situ hybridization and immunocytochemistry. |journal=Int. J. Cancer |volume=50 |issue= 2 |pages= 215-22 |year= 1992 |pmid= 1370435 |doi= }}
*{{cite journal | author=Zhou J, Bondy C |title=Insulin-like growth factor-II and its binding proteins in placental development. |journal=Endocrinology |volume=131 |issue= 3 |pages= 1230-40 |year= 1992 |pmid= 1380437 |doi= }}
*{{cite journal | author=Morgan DO, Edman JC, Standring DN, ''et al.'' |title=Insulin-like growth factor II receptor as a multifunctional binding protein. |journal=Nature |volume=329 |issue= 6137 |pages= 301-7 |year= 1987 |pmid= 2957598 |doi= 10.1038/329301a0 }}
*{{cite journal | author=Oshima A, Nolan CM, Kyle JW, ''et al.'' |title=The human cation-independent mannose 6-phosphate receptor. Cloning and sequence of the full-length cDNA and expression of functional receptor in COS cells. |journal=J. Biol. Chem. |volume=263 |issue= 5 |pages= 2553-62 |year= 1988 |pmid= 2963003 |doi= }}
*{{cite journal | author=De Souza AT, Hankins GR, Washington MK, ''et al.'' |title=M6P/IGF2R gene is mutated in human hepatocellular carcinomas with loss of heterozygosity. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 447-9 |year= 1996 |pmid= 7493029 |doi= 10.1038/ng1295-447 }}
*{{cite journal | author=Ilvesmäki V, Blum WF, Voutilainen R |title=Insulin-like growth factor binding proteins in the human adrenal gland. |journal=Mol. Cell. Endocrinol. |volume=97 |issue= 1-2 |pages= 71-9 |year= 1994 |pmid= 7511544 |doi= }}
*{{cite journal | author=De Souza AT, Hankins GR, Washington MK, ''et al.'' |title=Frequent loss of heterozygosity on 6q at the mannose 6-phosphate/insulin-like growth factor II receptor locus in human hepatocellular tumors. |journal=Oncogene |volume=10 |issue= 9 |pages= 1725-9 |year= 1995 |pmid= 7753549 |doi= }}
*{{cite journal | author=Schmidt B, Kiecke-Siemsen C, Waheed A, ''et al.'' |title=Localization of the insulin-like growth factor II binding site to amino acids 1508-1566 in repeat 11 of the mannose 6-phosphate/insulin-like growth factor II receptor. |journal=J. Biol. Chem. |volume=270 |issue= 25 |pages= 14975-82 |year= 1995 |pmid= 7797478 |doi= }}
*{{cite journal | author=Rao PH, Murty VV, Gaidano G, ''et al.'' |title=Subregional mapping of 8 single copy loci to chromosome 6 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=66 |issue= 4 |pages= 272-3 |year= 1994 |pmid= 8162705 |doi= }}
*{{cite journal | author=Ishiwata T, Bergmann U, Kornmann M, ''et al.'' |title=Altered expression of insulin-like growth factor II receptor in human pancreatic cancer. |journal=Pancreas |volume=15 |issue= 4 |pages= 367-73 |year= 1997 |pmid= 9361090 |doi= }}
*{{cite journal | author=Tikkanen R, Peltola M, Oinonen C, ''et al.'' |title=Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase. |journal=EMBO J. |volume=16 |issue= 22 |pages= 6684-93 |year= 1998 |pmid= 9362483 |doi= 10.1093/emboj/16.22.6684 }}
*{{cite journal | author=Nykjaer A, Christensen EI, Vorum H, ''et al.'' |title=Mannose 6-phosphate/insulin-like growth factor-II receptor targets the urokinase receptor to lysosomes via a novel binding interaction. |journal=J. Cell Biol. |volume=141 |issue= 3 |pages= 815-28 |year= 1998 |pmid= 9566979 |doi= }}
*{{cite journal | author=Díaz E, Pfeffer SR |title=TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. |journal=Cell |volume=93 |issue= 3 |pages= 433-43 |year= 1998 |pmid= 9590177 |doi= }}
*{{cite journal | author=Wan L, Molloy SS, Thomas L, ''et al.'' |title=PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization. |journal=Cell |volume=94 |issue= 2 |pages= 205-16 |year= 1998 |pmid= 9695949 |doi= }}
*{{cite journal | author=Killian JK, Jirtle RL |title=Genomic structure of the human M6P/IGF2 receptor. |journal=Mamm. Genome |volume=10 |issue= 1 |pages= 74-7 |year= 1999 |pmid= 9892739 |doi= }}
*{{cite journal | author=Kumar S, Hand AT, Connor JR, ''et al.'' |title=Identification and cloning of a connective tissue growth factor-like cDNA from human osteoblasts encoding a novel regulator of osteoblast functions. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 17123-31 |year= 1999 |pmid= 10358067 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITPR1... {November 14, 2007 5:46:51 PM PST}
- SEARCH REDIRECT: Control Box Found: ITPR1 {November 14, 2007 5:47:35 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:47:36 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:47:36 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:47:36 PM PST}
- UPDATED: Updated protein page: ITPR1 {November 14, 2007 5:47:42 PM PST}
- INFO: Beginning work on MSN... {November 14, 2007 5:47:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:48:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MSN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e5w.
| PDB = {{PDB2|1e5w}}, {{PDB2|1ef1}}, {{PDB2|1j19}}, {{PDB2|1sgh}}, {{PDB2|2d10}}, {{PDB2|2d11}}, {{PDB2|2d2q}}, {{PDB2|2yvc}}
| Name = Moesin
| HGNCid = 7373
| Symbol = MSN
| AltSymbols =;
| OMIM = 309845
| ECnumber =
| Homologene = 1833
| MGIid = 97167
| GeneAtlas_image1 = PBB_GE_MSN_200600_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0008092 |text = cytoskeletal protein binding}}
| Component = {{GNF_GO|id=GO:0001931 |text = uropod}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4478
| Hs_Ensembl = ENSG00000147065
| Hs_RefseqProtein = NP_002435
| Hs_RefseqmRNA = NM_002444
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 64804236
| Hs_GenLoc_end = 64878517
| Hs_Uniprot = P26038
| Mm_EntrezGene = 17698
| Mm_Ensembl = ENSMUSG00000031207
| Mm_RefseqmRNA = NM_010833
| Mm_RefseqProtein = NP_034963
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 92344584
| Mm_GenLoc_end = 92369353
| Mm_Uniprot = Q05DU4
}}
}}
'''Moesin''', also known as '''MSN''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Moesin (for membrane-organizing extension spike protein) is a member of the ERM family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons. Moesin is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and for cell movement.<ref>{{cite web | title = Entrez Gene: MSN moesin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4478| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tsukita S, Yonemura S |title=ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. |journal=Curr. Opin. Cell Biol. |volume=9 |issue= 1 |pages= 70-5 |year= 1997 |pmid= 9013673 |doi= }}
*{{cite journal | author=Vaheri A, Carpén O, Heiska L, ''et al.'' |title=The ezrin protein family: membrane-cytoskeleton interactions and disease associations. |journal=Curr. Opin. Cell Biol. |volume=9 |issue= 5 |pages= 659-66 |year= 1997 |pmid= 9330869 |doi= }}
*{{cite journal | author=Matarrese P, Malorni W |title=Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death. |journal=Cell Death Differ. |volume=12 Suppl 1 |issue= |pages= 932-41 |year= 2006 |pmid= 15818415 |doi= 10.1038/sj.cdd.4401582 }}
*{{cite journal | author=Lankes WT, Furthmayr H |title=Moesin: a member of the protein 4.1-talin-ezrin family of proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 19 |pages= 8297-301 |year= 1991 |pmid= 1924289 |doi= }}
*{{cite journal | author=Gary R, Bretscher A |title=Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. |journal=Mol. Biol. Cell |volume=6 |issue= 8 |pages= 1061-75 |year= 1995 |pmid= 7579708 |doi= }}
*{{cite journal | author=Schwartz-Albiez R, Merling A, Spring H, ''et al.'' |title=Differential expression of the microspike-associated protein moesin in human tissues. |journal=Eur. J. Cell Biol. |volume=67 |issue= 3 |pages= 189-98 |year= 1995 |pmid= 7588875 |doi= }}
*{{cite journal | author=Amieva MR, Furthmayr H |title=Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. |journal=Exp. Cell Res. |volume=219 |issue= 1 |pages= 180-96 |year= 1995 |pmid= 7628534 |doi= 10.1006/excr.1995.1218 }}
*{{cite journal | author=Schneider-Schaulies J, Dunster LM, Schwartz-Albiez R, ''et al.'' |title=Physical association of moesin and CD46 as a receptor complex for measles virus. |journal=J. Virol. |volume=69 |issue= 4 |pages= 2248-56 |year= 1995 |pmid= 7884872 |doi= }}
*{{cite journal | author=Wilgenbus KK, Hsieh CL, Lankes WT, ''et al.'' |title=Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN). |journal=Genomics |volume=19 |issue= 2 |pages= 326-33 |year= 1994 |pmid= 8188263 |doi= 10.1006/geno.1994.1065 }}
*{{cite journal | author=Gary R, Bretscher A |title=Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 22 |pages= 10846-50 |year= 1993 |pmid= 8248180 |doi= }}
*{{cite journal | author=Dunster LM, Schneider-Schaulies J, Löffler S, ''et al.'' |title=Moesin: a cell membrane protein linked with susceptibility to measles virus infection. |journal=Virology |volume=198 |issue= 1 |pages= 265-74 |year= 1994 |pmid= 8259662 |doi= }}
*{{cite journal | author=Nakamura F, Amieva MR, Furthmayr H |title=Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets. |journal=J. Biol. Chem. |volume=270 |issue= 52 |pages= 31377-85 |year= 1996 |pmid= 8537411 |doi= }}
*{{cite journal | author=Ott DE, Coren LV, Kane BP, ''et al.'' |title=Cytoskeletal proteins inside human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=70 |issue= 11 |pages= 7734-43 |year= 1996 |pmid= 8892894 |doi= }}
*{{cite journal | author=Hecker C, Weise C, Schneider-Schaulies J, ''et al.'' |title=Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin. |journal=Virus Res. |volume=49 |issue= 2 |pages= 215-23 |year= 1997 |pmid= 9213396 |doi= }}
*{{cite journal | author=Serrador JM, Alonso-Lebrero JL, del Pozo MA, ''et al.'' |title=Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization. |journal=J. Cell Biol. |volume=138 |issue= 6 |pages= 1409-23 |year= 1997 |pmid= 9298994 |doi= }}
*{{cite journal | author=Reczek D, Berryman M, Bretscher A |title=Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. |journal=J. Cell Biol. |volume=139 |issue= 1 |pages= 169-79 |year= 1998 |pmid= 9314537 |doi= }}
*{{cite journal | author=Murthy A, Gonzalez-Agosti C, Cordero E, ''et al.'' |title=NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1273-6 |year= 1998 |pmid= 9430655 |doi= }}
*{{cite journal | author=Yonemura S, Hirao M, Doi Y, ''et al.'' |title=Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. |journal=J. Cell Biol. |volume=140 |issue= 4 |pages= 885-95 |year= 1998 |pmid= 9472040 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR4A1... {November 14, 2007 5:44:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:45:28 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NR4A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cit.
| PDB = {{PDB2|1cit}}, {{PDB2|1yje}}, {{PDB2|2gbd}}
| Name = Nuclear receptor subfamily 4, group A, member 1
| HGNCid = 7980
| Symbol = NR4A1
| AltSymbols =; GFRP1; HMR; MGC9485; N10; NAK-1; NGFIB; NP10; NUR77; TR3
| OMIM = 139139
| ECnumber =
| Homologene = 1612
| MGIid = 1352454
| GeneAtlas_image1 = PBB_GE_NR4A1_202340_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_NR4A1_210226_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0004879 |text = ligand-dependent nuclear receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0043154 |text = negative regulation of caspase activity}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3164
| Hs_Ensembl = ENSG00000123358
| Hs_RefseqProtein = NP_002126
| Hs_RefseqmRNA = NM_002135
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 50717766
| Hs_GenLoc_end = 50739552
| Hs_Uniprot = P22736
| Mm_EntrezGene = 15370
| Mm_Ensembl = ENSMUSG00000023034
| Mm_RefseqmRNA = NM_010444
| Mm_RefseqProtein = NP_034574
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 101094887
| Mm_GenLoc_end = 101102826
| Mm_Uniprot = Q545Q1
}}
}}
'''Nuclear receptor subfamily 4, group A, member 1''', also known as '''NR4A1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the steroid-thyroid hormone-retinoid receptor superfamily. Expression is induced by phytohemagglutinin in human lymphocytes and by serum stimulation of arrested fibroblasts. The encoded protein acts as a nuclear transcription factor. Translocation of the protein from the nucleus to mitochondria induces apoptosis. Multiple alternatively spliced variants, encoding the same protein, have been identified.<ref>{{cite web | title = Entrez Gene: NR4A1 nuclear receptor subfamily 4, group A, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3164| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Winoto A, Littman DR |title=Nuclear hormone receptors in T lymphocytes. |journal=Cell |volume=109 Suppl |issue= |pages= S57-66 |year= 2002 |pmid= 11983153 |doi= }}
*{{cite journal | author=Engelse MA, Arkenbout EK, Pannekoek H, de Vries CJ |title=Activin and TR3 orphan receptor: two 'atheroprotective' genes as evidenced in dedicated mouse models. |journal=Clin. Exp. Pharmacol. Physiol. |volume=30 |issue= 11 |pages= 894-9 |year= 2004 |pmid= 14678255 |doi= }}
*{{cite journal | author=Bondy GP |title=Phorbol ester, forskolin, and serum induction of a human colon nuclear hormone receptor gene related to the NUR 77/NGFI-B genes. |journal=Cell Growth Differ. |volume=2 |issue= 4 |pages= 203-8 |year= 1991 |pmid= 1651101 |doi= }}
*{{cite journal | author=Nakai A, Kartha S, Sakurai A, ''et al.'' |title=A human early response gene homologous to murine nur77 and rat NGFI-B, and related to the nuclear receptor superfamily. |journal=Mol. Endocrinol. |volume=4 |issue= 10 |pages= 1438-43 |year= 1991 |pmid= 2283997 |doi= }}
*{{cite journal | author=Ryseck RP, Macdonald-Bravo H, Mattéi MG, ''et al.'' |title=Structure, mapping and expression of a growth factor inducible gene encoding a putative nuclear hormonal binding receptor. |journal=EMBO J. |volume=8 |issue= 11 |pages= 3327-35 |year= 1989 |pmid= 2555161 |doi= }}
*{{cite journal | author=Chang C, Kokontis J, Liao SS, Chang Y |title=Isolation and characterization of human TR3 receptor: a member of steroid receptor superfamily. |journal=J. Steroid Biochem. |volume=34 |issue= 1-6 |pages= 391-5 |year= 1990 |pmid= 2626032 |doi= }}
*{{cite journal | author=Uemura H, Mizokami A, Chang C |title=Identification of a new enhancer in the promoter region of human TR3 orphan receptor gene. A member of steroid receptor superfamily. |journal=J. Biol. Chem. |volume=270 |issue= 10 |pages= 5427-33 |year= 1995 |pmid= 7890657 |doi= }}
*{{cite journal | author=Hirata Y, Kiuchi K, Chen HC, ''et al.'' |title=The phosphorylation and DNA binding of the DNA-binding domain of the orphan nuclear receptor NGFI-B. |journal=J. Biol. Chem. |volume=268 |issue= 33 |pages= 24808-12 |year= 1993 |pmid= 8227042 |doi= }}
*{{cite journal | author=Harrison DC, Roberts J, Campbell CA, ''et al.'' |title=TR3 death receptor expression in the normal and ischaemic brain. |journal=Neuroscience |volume=96 |issue= 1 |pages= 147-60 |year= 2000 |pmid= 10777386 |doi= }}
*{{cite journal | author=Li H, Kolluri SK, Gu J, ''et al.'' |title=Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3. |journal=Science |volume=289 |issue= 5482 |pages= 1159-64 |year= 2000 |pmid= 10947977 |doi= }}
*{{cite journal | author=Pekarsky Y, Hallas C, Palamarchuk A, ''et al.'' |title=Akt phosphorylates and regulates the orphan nuclear receptor Nur77. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 7 |pages= 3690-4 |year= 2001 |pmid= 11274386 |doi= 10.1073/pnas.051003198 }}
*{{cite journal | author=Sohn YC, Kwak E, Na Y, ''et al.'' |title=Silencing mediator of retinoid and thyroid hormone receptors and activating signal cointegrator-2 as transcriptional coregulators of the orphan nuclear receptor Nur77. |journal=J. Biol. Chem. |volume=276 |issue= 47 |pages= 43734-9 |year= 2001 |pmid= 11559707 |doi= 10.1074/jbc.M107208200 }}
*{{cite journal | author=Lee MO, Kang HJ, Cho H, ''et al.'' |title=Hepatitis B virus X protein induced expression of the Nur77 gene. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 5 |pages= 1162-8 |year= 2001 |pmid= 11700033 |doi= 10.1006/bbrc.2001.5910 }}
*{{cite journal | author=Slagsvold HH, Østvold AC, Fallgren AB, Paulsen RE |title=Nuclear receptor and apoptosis initiator NGFI-B is a substrate for kinase ERK2. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 5 |pages= 1146-50 |year= 2002 |pmid= 11883936 |doi= 10.1006/bbrc.2002.6579 }}
*{{cite journal | author=Wu WS, Xu ZX, Ran R, ''et al.'' |title=Promyelocytic leukemia protein PML inhibits Nur77-mediated transcription through specific functional interactions. |journal=Oncogene |volume=21 |issue= 24 |pages= 3925-33 |year= 2002 |pmid= 12032831 |doi= 10.1038/sj.onc.1205491 }}
*{{cite journal | author=Liu S, Wu Q, Ye XF, ''et al.'' |title=Induction of apoptosis by TPA and VP-16 is through translocation of TR3. |journal=World J. Gastroenterol. |volume=8 |issue= 3 |pages= 446-50 |year= 2002 |pmid= 12046067 |doi= }}
*{{cite journal | author=Wansa KD, Harris JM, Muscat GE |title=The activation function-1 domain of Nur77/NR4A1 mediates trans-activation, cell specificity, and coactivator recruitment. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 33001-11 |year= 2002 |pmid= 12082103 |doi= 10.1074/jbc.M203572200 }}
*{{cite journal | author=Chtarbova S, Nimmrich I, Erdmann S, ''et al.'' |title=Murine Nr4a1 and Herpud1 are up-regulated by Wnt-1, but the homologous human genes are independent from beta-catenin activation. |journal=Biochem. J. |volume=367 |issue= Pt 3 |pages= 723-8 |year= 2002 |pmid= 12153396 |doi= 10.1042/BJ20020699 }}
*{{cite journal | author=Wu Q, Liu S, Ye XF, ''et al.'' |title=Dual roles of Nur77 in selective regulation of apoptosis and cell cycle by TPA and ATRA in gastric cancer cells. |journal=Carcinogenesis |volume=23 |issue= 10 |pages= 1583-92 |year= 2002 |pmid= 12376465 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on OLR1... {November 14, 2007 5:48:12 PM PST}
- SEARCH REDIRECT: Control Box Found: OLR1 {November 14, 2007 5:48:45 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:48:46 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:48:46 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:48:46 PM PST}
- UPDATED: Updated protein page: OLR1 {November 14, 2007 5:48:53 PM PST}
- INFO: Beginning work on PLA2G2A... {November 14, 2007 5:48:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:49:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PLA2G2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ayp.
| PDB = {{PDB2|1ayp}}, {{PDB2|1bbc}}, {{PDB2|1db4}}, {{PDB2|1db5}}, {{PDB2|1dcy}}, {{PDB2|1j1a}}, {{PDB2|1kqu}}, {{PDB2|1kvo}}, {{PDB2|1n28}}, {{PDB2|1n29}}, {{PDB2|1pod}}, {{PDB2|1poe}}
| Name = Phospholipase A2, group IIA (platelets, synovial fluid)
| HGNCid = 9031
| Symbol = PLA2G2A
| AltSymbols =; PLA2; MOM1; PLA2B; PLA2L; PLA2S; PLAS1; sPLA2
| OMIM = 172411
| ECnumber =
| Homologene = 254
| MGIid =
| GeneAtlas_image1 = PBB_GE_PLA2G2A_203649_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0047498 |text = calcium-dependent phospholipase A2 activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006644 |text = phospholipid metabolic process}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5320
| Hs_Ensembl = ENSG00000188257
| Hs_RefseqProtein = NP_000291
| Hs_RefseqmRNA = NM_000300
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 20174518
| Hs_GenLoc_end = 20179496
| Hs_Uniprot = P14555
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Phospholipase A2, group IIA (platelets, synovial fluid)''', also known as '''PLA2G2A''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kramer RM, Johansen B, Hession C, Pepinsky RB |title=Structure and properties of a secretable phospholipase A2 from human platelets. |journal=Adv. Exp. Med. Biol. |volume=275 |issue= |pages= 35-53 |year= 1990 |pmid= 2239446 |doi= }}
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4-5 |pages= 683-8 |year= 1998 |pmid= 9745929 |doi= }}
*{{cite journal | author=Law MH, Cotton RG, Berger GE |title=The role of phospholipases A2 in schizophrenia. |journal=Mol. Psychiatry |volume=11 |issue= 6 |pages= 547-56 |year= 2006 |pmid= 16585943 |doi= 10.1038/sj.mp.4001819 }}
*{{cite journal | author=Carlquist JF, Muhlestein JB, Anderson JL |title=Lipoprotein-associated phospholipase A2: a new biomarker for cardiovascular risk assessment and potential therapeutic target. |journal=Expert Rev. Mol. Diagn. |volume=7 |issue= 5 |pages= 511-7 |year= 2007 |pmid= 17892360 |doi= 10.1586/14737159.7.5.511 }}
*{{cite journal | author=Scott DL, White SP, Browning JL, ''et al.'' |title=Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. |journal=Science |volume=254 |issue= 5034 |pages= 1007-10 |year= 1991 |pmid= 1948070 |doi= }}
*{{cite journal | author=Pruzanski W, Bogoch E, Stefanski E, ''et al.'' |title=Enzymatic activity and distribution of phospholipase A2 in human cartilage. |journal=Life Sci. |volume=48 |issue= 25 |pages= 2457-62 |year= 1991 |pmid= 2046470 |doi= }}
*{{cite journal | author=Wery JP, Schevitz RW, Clawson DK, ''et al.'' |title=Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution. |journal=Nature |volume=352 |issue= 6330 |pages= 79-82 |year= 1991 |pmid= 2062381 |doi= 10.1038/352079a0 }}
*{{cite journal | author=Seilhamer JJ, Randall TL, Johnson LK, ''et al.'' |title=Novel gene exon homologous to pancreatic phospholipase A2: sequence and chromosomal mapping of both human genes. |journal=J. Cell. Biochem. |volume=39 |issue= 3 |pages= 327-37 |year= 1989 |pmid= 2708461 |doi= 10.1002/jcb.240390312 }}
*{{cite journal | author=Kanda A, Ono T, Yoshida N, ''et al.'' |title=The primary structure of a membrane-associated phospholipase A2 from human spleen. |journal=Biochem. Biophys. Res. Commun. |volume=163 |issue= 1 |pages= 42-8 |year= 1989 |pmid= 2775276 |doi= }}
*{{cite journal | author=Seilhamer JJ, Pruzanski W, Vadas P, ''et al.'' |title=Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. |journal=J. Biol. Chem. |volume=264 |issue= 10 |pages= 5335-8 |year= 1989 |pmid= 2925608 |doi= }}
*{{cite journal | author=Kramer RM, Hession C, Johansen B, ''et al.'' |title=Structure and properties of a human non-pancreatic phospholipase A2. |journal=J. Biol. Chem. |volume=264 |issue= 10 |pages= 5768-75 |year= 1989 |pmid= 2925633 |doi= }}
*{{cite journal | author=Lai CY, Wada K |title=Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 2 |pages= 488-93 |year= 1989 |pmid= 3202859 |doi= }}
*{{cite journal | author=Hara S, Kudo I, Matsuta K, ''et al.'' |title=Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid. |journal=J. Biochem. |volume=104 |issue= 3 |pages= 326-8 |year= 1989 |pmid= 3240982 |doi= }}
*{{cite journal | author=Schevitz RW, Bach NJ, Carlson DG, ''et al.'' |title=Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2. |journal=Nat. Struct. Biol. |volume=2 |issue= 6 |pages= 458-65 |year= 1995 |pmid= 7664108 |doi= }}
*{{cite journal | author=Ancian P, Lambeau G, Mattéi MG, Lazdunski M |title=The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization. |journal=J. Biol. Chem. |volume=270 |issue= 15 |pages= 8963-70 |year= 1995 |pmid= 7721806 |doi= }}
*{{cite journal | author=MacPhee M, Chepenik KP, Liddell RA, ''et al.'' |title=The secretory phospholipase A2 gene is a candidate for the Mom1 locus, a major modifier of ApcMin-induced intestinal neoplasia. |journal=Cell |volume=81 |issue= 6 |pages= 957-66 |year= 1995 |pmid= 7781071 |doi= }}
*{{cite journal | author=Minami T, Tojo H, Shinomura Y, ''et al.'' |title=Purification and characterization of a phospholipase A2 from human ileal mucosa. |journal=Biochim. Biophys. Acta |volume=1170 |issue= 2 |pages= 125-30 |year= 1993 |pmid= 8399335 |doi= }}
*{{cite journal | author=Sartipy P, Johansen B, Camejo G, ''et al.'' |title=Binding of human phospholipase A2 type II to proteoglycans. Differential effect of glycosaminoglycans on enzyme activity. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26307-14 |year= 1996 |pmid= 8824283 |doi= }}
*{{cite journal | author=Tischfield JA, Xia YR, Shih DM, ''et al.'' |title=Low-molecular-weight, calcium-dependent phospholipase A2 genes are linked and map to homologous chromosome regions in mouse and human. |journal=Genomics |volume=32 |issue= 3 |pages= 328-33 |year= 1997 |pmid= 8838795 |doi= 10.1006/geno.1996.0126 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRSS1... {November 14, 2007 5:49:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:50:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PRSS1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1trn.
| PDB = {{PDB2|1trn}}
| Name = Protease, serine, 1 (trypsin 1)
| HGNCid = 9475
| Symbol = PRSS1
| AltSymbols =; MGC120175; MGC149362; TRP1; TRY1; TRY4; TRYP1
| OMIM = 276000
| ECnumber =
| Homologene = 68276
| MGIid = 3687012
| GeneAtlas_image1 = PBB_GE_PRSS1_205869_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0004295 |text = trypsin activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007586 |text = digestion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5644
| Hs_Ensembl = ENSG00000173636
| Hs_RefseqProtein = NP_002760
| Hs_RefseqmRNA = NM_002769
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 142136904
| Hs_GenLoc_end = 142140495
| Hs_Uniprot = P07477
| Mm_EntrezGene = 386551
| Mm_Ensembl = ENSMUSG00000059014
| Mm_RefseqmRNA = NM_001003664
| Mm_RefseqProtein = NP_001003664
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 41344917
| Mm_GenLoc_end = 41430791
| Mm_Uniprot =
}}
}}
'''Protease, serine, 1 (trypsin 1)''', also known as '''PRSS1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active form in the small intestine. It is active on peptide linkages involving the carboxyl group of lysine or arginine. Mutations in this gene are associated with hereditary pancreatitis. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7.<ref>{{cite web | title = Entrez Gene: PRSS1 protease, serine, 1 (trypsin 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5644| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chen JM, Ferec C |title=Molecular basis of hereditary pancreatitis. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 7 |pages= 473-9 |year= 2000 |pmid= 10909845 |doi= 10.1038/sj.ejhg.5200492 }}
*{{cite journal | author=Chen JM, Ferec C |title=Gene conversion-like missense mutations in the human cationic trypsinogen gene and insights into the molecular evolution of the human trypsinogen family. |journal=Mol. Genet. Metab. |volume=71 |issue= 3 |pages= 463-9 |year= 2000 |pmid= 11073713 |doi= 10.1006/mgme.2000.3086 }}
*{{cite journal | author=Chen JM, Montier T, Férec C |title=Molecular pathology and evolutionary and physiological implications of pancreatitis-associated cationic trypsinogen mutations. |journal=Hum. Genet. |volume=109 |issue= 3 |pages= 245-52 |year= 2001 |pmid= 11702203 |doi= 10.1007/s004390100580 }}
*{{cite journal | author=Howes N, Greenhalf W, Stocken DD, Neoptolemos JP |title=Cationic trypsinogen mutations and pancreatitis. |journal=Clin. Lab. Med. |volume=25 |issue= 1 |pages= 39-59 |year= 2005 |pmid= 15749231 |doi= 10.1016/j.cll.2004.12.004 }}
*{{cite journal | author=Kandula L, Whitcomb DC, Lowe ME |title=Genetic issues in pediatric pancreatitis. |journal=Current gastroenterology reports |volume=8 |issue= 3 |pages= 248-53 |year= 2006 |pmid= 16764792 |doi= }}
*{{cite journal | author=Yamamoto KK, Pousette A, Chow P, ''et al.'' |title=Isolation of a cDNA encoding a human serum marker for acute pancreatitis. Identification of pancreas-specific protein as pancreatic procarboxypeptidase B. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2575-81 |year= 1992 |pmid= 1370825 |doi= }}
*{{cite journal | author=Pollard SR, Meier W, Chow P, ''et al.'' |title=CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11320-4 |year= 1992 |pmid= 1763044 |doi= }}
*{{cite journal | author=Shieh BH, Travis J |title=The reactive site of human alpha 2-antiplasmin. |journal=J. Biol. Chem. |volume=262 |issue= 13 |pages= 6055-9 |year= 1987 |pmid= 2437112 |doi= }}
*{{cite journal | author=Kimland M, Russick C, Marks WH, Borgström A |title=Immunoreactive anionic and cationic trypsin in human serum. |journal=Clin. Chim. Acta |volume=184 |issue= 1 |pages= 31-46 |year= 1990 |pmid= 2598466 |doi= }}
*{{cite journal | author=Emi M, Nakamura Y, Ogawa M, ''et al.'' |title=Cloning, characterization and nucleotide sequences of two cDNAs encoding human pancreatic trypsinogens. |journal=Gene |volume=41 |issue= 2-3 |pages= 305-10 |year= 1986 |pmid= 3011602 |doi= }}
*{{cite journal | author=Honey NK, Sakaguchi AY, Quinto C, ''et al.'' |title=Chromosomal assignments of human genes for serine proteases trypsin, chymotrypsin B, and elastase. |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 4 |pages= 369-76 |year= 1984 |pmid= 6589790 |doi= }}
*{{cite journal | author=Merrill GA, Butler M, Horowitz PM |title=Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding. |journal=J. Biol. Chem. |volume=268 |issue= 21 |pages= 15611-20 |year= 1993 |pmid= 8340386 |doi= }}
*{{cite journal | author=Rowen L, Koop BF, Hood L |title=The complete 685-kilobase DNA sequence of the human beta T cell receptor locus. |journal=Science |volume=272 |issue= 5269 |pages= 1755-62 |year= 1996 |pmid= 8650574 |doi= }}
*{{cite journal | author=Gaboriaud C, Serre L, Guy-Crotte O, ''et al.'' |title=Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151. |journal=J. Mol. Biol. |volume=259 |issue= 5 |pages= 995-1010 |year= 1996 |pmid= 8683601 |doi= 10.1006/jmbi.1996.0376 }}
*{{cite journal | author=Whitcomb DC, Gorry MC, Preston RA, ''et al.'' |title=Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 141-5 |year= 1996 |pmid= 8841182 |doi= 10.1038/ng1096-141 }}
*{{cite journal | author=Gu M, Majerus PW |title=The properties of the protein tyrosine phosphatase PTPMEG. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27751-9 |year= 1996 |pmid= 8910369 |doi= }}
*{{cite journal | author=Christensen S, Valnickova Z, Thogersen IB, ''et al.'' |title=Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional properties. |journal=Biochem. J. |volume=323 ( Pt 3) |issue= |pages= 847-52 |year= 1997 |pmid= 9169621 |doi= }}
*{{cite journal | author=Gorry MC, Gabbaizedeh D, Furey W, ''et al.'' |title=Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis. |journal=Gastroenterology |volume=113 |issue= 4 |pages= 1063-8 |year= 1997 |pmid= 9322498 |doi= }}
*{{cite journal | author=Dahlen JR, Foster DC, Kisiel W |title=Expression, purification, and inhibitory properties of human proteinase inhibitor. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14874-82 |year= 1998 |pmid= 9402754 |doi= 10.1021/bi970977p }}
*{{cite journal | author=Teich N, Mössner J, Keim V |title=Mutations of the cationic trypsinogen in hereditary pancreatitis. |journal=Hum. Mutat. |volume=12 |issue= 1 |pages= 39-43 |year= 1998 |pmid= 9633818 |doi= 10.1002/(SICI)1098-1004(1998)12:1<39::AID-HUMU6>3.0.CO;2-P }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRTN3... {November 14, 2007 5:50:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:50:47 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PRTN3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fuj.
| PDB = {{PDB2|1fuj}}
| Name = Proteinase 3 (serine proteinase, neutrophil, Wegener granulomatosis autoantigen)
| HGNCid = 9495
| Symbol = PRTN3
| AltSymbols =; ACPA; AGP7; C-ANCA; MBT; P29; PR-3
| OMIM = 177020
| ECnumber =
| Homologene = 20615
| MGIid = 893580
| GeneAtlas_image1 = PBB_GE_PRTN3_207341_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030574 |text = collagen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5657
| Hs_Ensembl = ENSG00000196415
| Hs_RefseqProtein = NP_002768
| Hs_RefseqmRNA = NM_002777
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 791985
| Hs_GenLoc_end = 799175
| Hs_Uniprot = P24158
| Mm_EntrezGene = 19152
| Mm_Ensembl = ENSMUSG00000057729
| Mm_RefseqmRNA = NM_011178
| Mm_RefseqProtein = NP_035308
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 79282796
| Mm_GenLoc_end = 79286303
| Mm_Uniprot = Q61096
}}
}}
'''Proteinase 3 (serine proteinase, neutrophil, Wegener granulomatosis autoantigen)''', also known as '''PRTN3''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Watorek E, Boratyńska M, Klinger M |title=Wegener's granulomatosis--autoimmunity to neutrophil proteinase 3. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=51 |issue= 3 |pages= 157-67 |year= 2004 |pmid= 12894870 |doi= }}
*{{cite journal | author=van der Helm-van Mil AH, Huizinga TW, de Vries RR, Toes RE |title=Emerging patterns of risk factor make-up enable subclassification of rheumatoid arthritis. |journal=Arthritis Rheum. |volume=56 |issue= 6 |pages= 1728-35 |year= 2007 |pmid= 17534941 |doi= 10.1002/art.22716 }}
*{{cite journal | author=Sturrock AB, Franklin KF, Rao G, ''et al.'' |title=Structure, chromosomal assignment, and expression of the gene for proteinase-3. The Wegener's granulomatosis autoantigen. |journal=J. Biol. Chem. |volume=267 |issue= 29 |pages= 21193-9 |year= 1992 |pmid= 1400430 |doi= }}
*{{cite journal | author=Zimmer M, Medcalf RL, Fink TM, ''et al.'' |title=Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 8215-9 |year= 1992 |pmid= 1518849 |doi= }}
*{{cite journal | author=Labbaye C, Musette P, Cayre YE |title=Wegener autoantigen and myeloblastin are encoded by a single mRNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 20 |pages= 9253-6 |year= 1991 |pmid= 1681549 |doi= }}
*{{cite journal | author=Lüdemann J, Utecht B, Gross WL |title=Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme. |journal=J. Exp. Med. |volume=171 |issue= 1 |pages= 357-62 |year= 1990 |pmid= 1688612 |doi= }}
*{{cite journal | author=Musette P, Labbaye C, Dorner MH, ''et al.'' |title=Wegener's autoantigen and leukemia. |journal=Blood |volume=77 |issue= 6 |pages= 1398-9 |year= 1991 |pmid= 2001463 |doi= }}
*{{cite journal | author=Rao NV, Wehner NG, Marshall BC, ''et al.'' |title=Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties. |journal=J. Biol. Chem. |volume=266 |issue= 15 |pages= 9540-8 |year= 1991 |pmid= 2033050 |doi= }}
*{{cite journal | author=Ohlsson K, Linder C, Rosengren M |title=Monoclonal antibodies specific for neutrophil proteinase 4. Production and use for isolation of the enzyme. |journal=Biol. Chem. Hoppe-Seyler |volume=371 |issue= 7 |pages= 549-55 |year= 1990 |pmid= 2121162 |doi= }}
*{{cite journal | author=Gupta SK, Niles JL, McCluskey RT, Arnaout MA |title=Identity of Wegener's autoantigen (p29) with proteinase 3 and myeloblastin. |journal=Blood |volume=76 |issue= 10 |pages= 2162 |year= 1990 |pmid= 2242436 |doi= }}
*{{cite journal | author=Campanelli D, Melchior M, Fu Y, ''et al.'' |title=Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils. |journal=J. Exp. Med. |volume=172 |issue= 6 |pages= 1709-15 |year= 1991 |pmid= 2258701 |doi= }}
*{{cite journal | author=Goldschmeding R, Dolman KM, van den Ende ME, ''et al.'' |title=The relation of 29 kD C-ANCA antigen to proteinase 3. |journal=APMIS Suppl. |volume=19 |issue= |pages= 26-7 |year= 1991 |pmid= 2285532 |doi= }}
*{{cite journal | author=Jenne DE, Tschopp J, Lüdemann J, ''et al.'' |title=Wegener's autoantigen decoded. |journal=Nature |volume=346 |issue= 6284 |pages= 520 |year= 1990 |pmid= 2377228 |doi= 10.1038/346520a0 }}
*{{cite journal | author=Wilde CG, Snable JL, Griffith JE, Scott RW |title=Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase. |journal=J. Biol. Chem. |volume=265 |issue= 4 |pages= 2038-41 |year= 1990 |pmid= 2404977 |doi= }}
*{{cite journal | author=Gabay JE, Scott RW, Campanelli D, ''et al.'' |title=Antibiotic proteins of human polymorphonuclear leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5610-4 |year= 1989 |pmid= 2501794 |doi= }}
*{{cite journal | author=Bories D, Raynal MC, Solomon DH, ''et al.'' |title=Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells. |journal=Cell |volume=59 |issue= 6 |pages= 959-68 |year= 1990 |pmid= 2598267 |doi= }}
*{{cite journal | author=Niles JL, McCluskey RT, Ahmad MF, Arnaout MA |title=Wegener's granulomatosis autoantigen is a novel neutrophil serine proteinase. |journal=Blood |volume=74 |issue= 6 |pages= 1888-93 |year= 1989 |pmid= 2679910 |doi= }}
*{{cite journal | author=Pontremoli S, Melloni E, Michetti M, ''et al.'' |title=Cytolytic effects of neutrophils: role for a membrane-bound neutral proteinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 6 |pages= 1685-9 |year= 1986 |pmid= 3513185 |doi= }}
*{{cite journal | author=Sugimori T, Cooley J, Hoidal JR, Remold-O'Donnell E |title=Inhibitory properties of recombinant human monocyte/neutrophil elastase inhibitor. |journal=Am. J. Respir. Cell Mol. Biol. |volume=13 |issue= 3 |pages= 314-22 |year= 1995 |pmid= 7654387 |doi= }}
*{{cite journal | author=Muller-Bérat N, Minowada J, Tsuji-Takayama K, ''et al.'' |title=The phylogeny of proteinase 3/myeloblastin, the autoantigen in Wegener's granulomatosis, and myeloperoxidase as shown by immunohistochemical studies on human leukemic cell lines. |journal=Clin. Immunol. Immunopathol. |volume=70 |issue= 1 |pages= 51-9 |year= 1994 |pmid= 8261669 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TOR1A... {November 14, 2007 5:40:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:41:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Torsin family 1, member A (torsin A)
| HGNCid = 3098
| Symbol = TOR1A
| AltSymbols =; DQ2; DYT1; torsin A
| OMIM = 605204
| ECnumber =
| Homologene = 37263
| MGIid = 1353568
| GeneAtlas_image1 = PBB_GE_TOR1A_202348_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TOR1A_202349_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008462 |text = endopeptidase Clp activity}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}} {{GNF_GO|id=GO:0051085 |text = chaperone cofactor-dependent protein folding}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1861
| Hs_Ensembl = ENSG00000136827
| Hs_RefseqProtein = NP_000104
| Hs_RefseqmRNA = NM_000113
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 131615043
| Hs_GenLoc_end = 131626234
| Hs_Uniprot = O14656
| Mm_EntrezGene = 30931
| Mm_Ensembl = ENSMUSG00000026849
| Mm_RefseqmRNA = NM_144884
| Mm_RefseqProtein = NP_659133
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 30782636
| Mm_GenLoc_end = 30789942
| Mm_Uniprot = Q3TV62
}}
}}
'''Torsin family 1, member A (torsin A)''', also known as '''TOR1A''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the AAA family of adenosine triphosphatases (ATPases), is related to the Clp protease/heat shock family and is expressed prominently in the substantia nigra pars compacta. Mutations in this gene result in the autosomal dominant disorder, torsion dystonia 1.<ref>{{cite web | title = Entrez Gene: TOR1A torsin family 1, member A (torsin A)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1861| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ozelius LJ, Hewett JW, Page CE, ''et al.'' |title=The gene (DYT1) for early-onset torsion dystonia encodes a novel protein related to the Clp protease/heat shock family. |journal=Advances in neurology |volume=78 |issue= |pages= 93-105 |year= 1998 |pmid= 9750906 |doi= }}
*{{cite journal | author=Ferrari Toninelli G, Spano P, Memo M |title=TorsinA, microtubules and cell polarity. |journal=Funct. Neurol. |volume=18 |issue= 1 |pages= 7-10 |year= 2003 |pmid= 12760408 |doi= }}
*{{cite journal | author=Rothwell JC, Edwards M, Huang YZ, Bhatia KP |title=Physiological studies in carriers of the DYT1 gene mutation. |journal=Rev. Neurol. (Paris) |volume=159 |issue= 10 Pt 1 |pages= 880-4 |year= 2004 |pmid= 14615676 |doi= }}
*{{cite journal | author=Ozelius LJ, Hewett JW, Page CE, ''et al.'' |title=The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 40-8 |year= 1997 |pmid= 9288096 |doi= 10.1038/ng0997-40 }}
*{{cite journal | author=Augood SJ, Penney JB, Friberg IK, ''et al.'' |title=Expression of the early-onset torsion dystonia gene (DYT1) in human brain. |journal=Ann. Neurol. |volume=43 |issue= 5 |pages= 669-73 |year= 1998 |pmid= 9585364 |doi= 10.1002/ana.410430518 }}
*{{cite journal | author=Kamm C, Castelon-Konkiewitz E, Naumann M, ''et al.'' |title=GAG deletion in the DYT1 gene in early limb-onset idiopathic torsion dystonia in Germany. |journal=Mov. Disord. |volume=14 |issue= 4 |pages= 681-3 |year= 1999 |pmid= 10435508 |doi= }}
*{{cite journal | author=Ikeuchi T, Shimohata T, Nakano R, ''et al.'' |title=A case of primary torsion dystonia in Japan with the 3-bp (GAG) deletion in the DYT1 gene with a unique clinical presentation. |journal=Neurogenetics |volume=2 |issue= 3 |pages= 189-90 |year= 1999 |pmid= 10541594 |doi= }}
*{{cite journal | author=Shashidharan P, Kramer BC, Walker RH, ''et al.'' |title=Immunohistochemical localization and distribution of torsinA in normal human and rat brain. |journal=Brain Res. |volume=853 |issue= 2 |pages= 197-206 |year= 2000 |pmid= 10640617 |doi= }}
*{{cite journal | author=Ozelius LJ, Page CE, Klein C, ''et al.'' |title=The TOR1A (DYT1) gene family and its role in early onset torsion dystonia. |journal=Genomics |volume=62 |issue= 3 |pages= 377-84 |year= 2000 |pmid= 10644435 |doi= 10.1006/geno.1999.6039 }}
*{{cite journal | author=Hewett J, Gonzalez-Agosti C, Slater D, ''et al.'' |title=Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells. |journal=Hum. Mol. Genet. |volume=9 |issue= 9 |pages= 1403-13 |year= 2000 |pmid= 10814722 |doi= }}
*{{cite journal | author=Kustedjo K, Bracey MH, Cravatt BF |title=Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 27933-9 |year= 2000 |pmid= 10871631 |doi= 10.1074/jbc.M910025199 }}
*{{cite journal | author=Suzuki Y, Tsunoda T, Sese J, ''et al.'' |title=Identification and characterization of the potential promoter regions of 1031 kinds of human genes. |journal=Genome Res. |volume=11 |issue= 5 |pages= 677-84 |year= 2001 |pmid= 11337467 |doi= 10.1101/gr.164001 }}
*{{cite journal | author=Konakova M, Huynh DP, Yong W, Pulst SM |title=Cellular distribution of torsin A and torsin B in normal human brain. |journal=Arch. Neurol. |volume=58 |issue= 6 |pages= 921-7 |year= 2001 |pmid= 11405807 |doi= }}
*{{cite journal | author=Sharma N, Hewett J, Ozelius LJ, ''et al.'' |title=A close association of torsinA and alpha-synuclein in Lewy bodies: a fluorescence resonance energy transfer study. |journal=Am. J. Pathol. |volume=159 |issue= 1 |pages= 339-44 |year= 2001 |pmid= 11438481 |doi= }}
*{{cite journal | author=Leung JC, Klein C, Friedman J, ''et al.'' |title=Novel mutation in the TOR1A (DYT1) gene in atypical early onset dystonia and polymorphisms in dystonia and early onset parkinsonism. |journal=Neurogenetics |volume=3 |issue= 3 |pages= 133-43 |year= 2002 |pmid= 11523564 |doi= }}
*{{cite journal | author=Tuffery-Giraud S, Cavalier L, Roubertie A, ''et al.'' |title=No evidence of allelic heterogeneity in the DYT1 gene of European patients with early onset torsion dystonia. |journal=J. Med. Genet. |volume=38 |issue= 10 |pages= E35 |year= 2002 |pmid= 11584049 |doi= }}
*{{cite journal | author=Major T, Svetel M, Romac S, Kostić VS |title=DYT1 mutation in primary torsion dystonia in a Serbian population. |journal=J. Neurol. |volume=248 |issue= 11 |pages= 940-3 |year= 2002 |pmid= 11757956 |doi= }}
*{{cite journal | author=Walker RH, Morgello S, Davidoff-Feldman B, ''et al.'' |title=Autosomal dominant chorea-acanthocytosis with polyglutamine-containing neuronal inclusions. |journal=Neurology |volume=58 |issue= 7 |pages= 1031-7 |year= 2002 |pmid= 11940688 |doi= }}
*{{cite journal | author=Hjermind LE, Werdelin LM, Sørensen SA |title=Inherited and de novo mutations in sporadic cases of DYT1-dystonia. |journal=Eur. J. Hum. Genet. |volume=10 |issue= 3 |pages= 213-6 |year= 2002 |pmid= 11973627 |doi= 10.1038/sj.ejhg.5200782 }}
}}
{{refend}}
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